Rhodopsin: A purplish-red, light-sensitive pigment found in RETINAL ROD CELLS of most vertebrates. It is a complex consisting of a molecule of ROD OPSIN and a molecule of 11-cis retinal (RETINALDEHYDE). Rhodopsin exhibits peak absorption wavelength at about 500 nm.Opsins: Photosensitive proteins in the membranes of PHOTORECEPTOR CELLS such as the rods and the cones. Opsins have varied light absorption properties and are members of the G-PROTEIN-COUPLED RECEPTORS family. Their ligands are VITAMIN A-based chromophores.Rod Opsins: Photosensitive proteins expressed in the ROD PHOTORECEPTOR CELLS. They are the protein components of rod photoreceptor pigments such as RHODOPSIN.Cone Opsins: Photosensitive proteins expressed in the CONE PHOTORECEPTOR CELLS. They are the protein components of cone photopigments. Cone opsins are classified by their peak absorption wavelengths.Sensory Rhodopsins: Photosensory rhodopsins found in microorganisms such as HALOBACTERIA. They convert light signals into biochemical information that regulates certain cellular functions such as flagellar motor activity.Retinal Pigments: Photosensitive protein complexes of varied light absorption properties which are expressed in the PHOTORECEPTOR CELLS. They are OPSINS conjugated with VITAMIN A-based chromophores. Chromophores capture photons of light, leading to the activation of opsins and a biochemical cascade that ultimately excites the photoreceptor cells.Rhodopsins, Microbial: Rhodopsin molecules found in microorganisms such as ARCHAEA and PROTEOBACTERIA.G-Protein-Coupled Receptor Kinase 1: A PROTEIN-SERINE-THREONINE KINASE that is found in PHOTORECEPTOR CELLS. It mediates light-dependent PHOSPHORYLATION of RHODOPSIN and plays an important role in PHOTOTRANSDUCTION.Retinaldehyde: A carotenoid constituent of visual pigments. It is the oxidized form of retinol which functions as the active component of the visual cycle. It is bound to the protein opsin forming the complex rhodopsin. When stimulated by visible light, the retinal component of the rhodopsin complex undergoes isomerization at the 11-position of the double bond to the cis-form; this is reversed in "dark" reactions to return to the native trans-configuration.Transducin: A heterotrimeric GTP-binding protein that mediates the light activation signal from photolyzed rhodopsin to cyclic GMP phosphodiesterase and is pivotal in the visual excitation process. Activation of rhodopsin on the outer membrane of rod and cone cells causes GTP to bind to transducin followed by dissociation of the alpha subunit-GTP complex from the beta/gamma subunits of transducin. The alpha subunit-GTP complex activates the cyclic GMP phosphodiesterase which catalyzes the hydrolysis of cyclic GMP to 5'-GMP. This leads to closure of the sodium and calcium channels and therefore hyperpolarization of the rod cells. EC 3.6.1.-.Rod Cell Outer Segment: The portion of a retinal rod cell situated between the ROD INNER SEGMENT and the RETINAL PIGMENT EPITHELIUM. It contains a stack of photosensitive disk membranes laden with RHODOPSIN.Light: That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.Retinal Rod Photoreceptor Cells: Photosensitive afferent neurons located in the peripheral retina, with their density increases radially away from the FOVEA CENTRALIS. Being much more sensitive to light than the RETINAL CONE CELLS, the rod cells are responsible for twilight vision (at scotopic intensities) as well as peripheral vision, but provide no color discrimination.Photoreceptor Cells: Specialized cells that detect and transduce light. They are classified into two types based on their light reception structure, the ciliary photoreceptors and the rhabdomeric photoreceptors with MICROVILLI. Ciliary photoreceptor cells use OPSINS that activate a PHOSPHODIESTERASE phosphodiesterase cascade. Rhabdomeric photoreceptor cells use opsins that activate a PHOSPHOLIPASE C cascade.Retinal Cone Photoreceptor Cells: Photosensitive afferent neurons located primarily within the FOVEA CENTRALIS of the MACULA LUTEA. There are three major types of cone cells (red, blue, and green) whose photopigments have different spectral sensitivity curves. Retinal cone cells operate in daylight vision (at photopic intensities) providing color recognition and central visual acuity.Vision, Ocular: The process in which light signals are transformed by the PHOTORECEPTOR CELLS into electrical signals which can then be transmitted to the brain.Eye ProteinsRetina: The ten-layered nervous tissue membrane of the eye. It is continuous with the OPTIC NERVE and receives images of external objects and transmits visual impulses to the brain. Its outer surface is in contact with the CHOROID and the inner surface with the VITREOUS BODY. The outer-most layer is pigmented, whereas the inner nine layers are transparent.Photoreceptor Cells, Invertebrate: Specialized cells in the invertebrates that detect and transduce light. They are predominantly rhabdomeric with an array of photosensitive microvilli. Illumination depolarizes invertebrate photoreceptors by stimulating Na+ influx across the plasma membrane.Photoreceptor Cells, Vertebrate: Specialized PHOTOTRANSDUCTION neurons in the vertebrates, such as the RETINAL ROD CELLS and the RETINAL CONE CELLS. Non-visual photoreceptor neurons have been reported in the deep brain, the PINEAL GLAND and organs of the circadian system.Microspectrophotometry: Analytical technique for studying substances present at enzyme concentrations in single cells, in situ, by measuring light absorption. Light from a tungsten strip lamp or xenon arc dispersed by a grating monochromator illuminates the optical system of a microscope. The absorbance of light is measured (in nanometers) by comparing the difference between the image of the sample and a reference image.Dark Adaptation: Adjustment of the eyes under conditions of low light. The sensitivity of the eye to light is increased during dark adaptation.Retinitis Pigmentosa: Hereditary, progressive degeneration of the neuroepithelium of the retina characterized by night blindness and progressive contraction of the visual field.Halorhodopsins: Light driven chloride ion pumps that are ubiquitously found in halophilic archaea (HALOBACTERIALES).Light Signal Transduction: The conversion of absorbed light energy into molecular signals.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Schiff Bases: Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)Retinal Degeneration: A retrogressive pathological change in the retina, focal or generalized, caused by genetic defects, inflammation, trauma, vascular disease, or aging. Degeneration affecting predominantly the macula lutea of the retina is MACULAR DEGENERATION. (Newell, Ophthalmology: Principles and Concepts, 7th ed, p304)Electroretinography: Recording of electric potentials in the retina after stimulation by light.Recoverin: A neuronal calcium-sensor protein that is found in ROD PHOTORECEPTORS and CONE PHOTORECEPTORS. It interacts with G-PROTEIN-COUPLED RECEPTOR KINASE 1 in a Ca2+ dependent manner and plays an important role in PHOTOTRANSDUCTION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Compound Eye, Arthropod: Light sensory organ in ARTHROPODS consisting of a large number of ommatidia, each functioning as an independent photoreceptor unit.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Octopodiformes: A superorder in the class CEPHALOPODA, consisting of the orders Octopoda (octopus) with over 200 species and Vampyromorpha with a single species. The latter is a phylogenetic relic but holds the key to the origins of Octopoda.Natronobacterium: A genus of rod-shaped, extremely halophilic HALOBACTERIACEAE which grows in alkaline conditions. They are strictly aerobic and some strains are motile. Natronobacterium is found in soda lakes, alkaline salterns, and soda soils.Hippocalcin: A neuronal calcium-sensor protein that was initially found in the NEURONS of the HIPPOCAMPUS. It interacts with NEURONAL APOPTOSIS-INHIBITORY PROTEIN.PhotochemistryBacteriorhodopsins: Rhodopsins found in the PURPLE MEMBRANE of halophilic archaea such as HALOBACTERIUM HALOBIUM. Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS.Hydrozoa: A class in the phylum CNIDARIA which alternates between polyp and medusa forms during their life cycle. There are over 2700 species in five orders.Darkness: The absence of light.Hydroxylamine: A colorless inorganic compound (HONH2) used in organic synthesis and as a reducing agent, due to its ability to donate nitric oxide.Cichlids: Common name for perch-like fish of the family Cichlidae, belonging to the suborder Labroidei, order PERCIFORMES.Color Vision: Function of the human eye that is used in bright illumination or in daylight (at photopic intensities). Photopic vision is performed by the three types of RETINAL CONE PHOTORECEPTORS with varied peak absorption wavelengths in the color spectrum (from violet to red, 400 - 700 nm).Poecilia: A genus of livebearing cyprinodont fish comprising the guppy and molly. Some species are virtually all female and depend on sperm from other species to stimulate egg development. Poecilia is used in carcinogenicity studies as well as neurologic and physiologic research.Eye: The organ of sight constituting a pair of globular organs made up of a three-layered roughly spherical structure specialized for receiving and responding to light.Pineal Gland: A light-sensitive neuroendocrine organ attached to the roof of the THIRD VENTRICLE of the brain. The pineal gland secretes MELATONIN, other BIOGENIC AMINES and NEUROPEPTIDES.Butterflies: Slender-bodies diurnal insects having large, broad wings often strikingly colored and patterned.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Spectrum Analysis: The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Photolysis: Chemical bond cleavage reactions resulting from absorption of radiant energy.Drug Inverse Agonism: Phenomena and pharmaceutics of compounds that bind to the same receptor binding-site as an agonist (DRUG AGONISM) for that receptor but exerts the opposite pharmacological effect.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Night Blindness: Failure or imperfection of vision at night or in dim light, with good vision only on bright days. (Dorland, 27th ed)Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Crustacea: A large subphylum of mostly marine ARTHROPODS containing over 42,000 species. They include familiar arthropods such as lobsters (NEPHROPIDAE), crabs (BRACHYURA), shrimp (PENAEIDAE), and barnacles (THORACICA).Cyprinodontiformes: An order of fish with eight families and numerous species of both egg-laying and livebearing fish. Families include Cyprinodontidae (egg-laying KILLIFISHES;), FUNDULIDAEl; (topminnows), Goodeidae (Mexican livebearers), Jenynsiidae (jenynsiids), Poeciliidae (livebearers), Profundulidae (Middle American killifishes), Aplocheilidae, and Rivulidae (rivulines). In the family Poeciliidae, the guppy and molly belong to the genus POECILIA.Halobacterium salinarum: A species of halophilic archaea found in salt lakes. Some strains form a PURPLE MEMBRANE under anaerobic conditions.Hydroxylamines: Organic compounds that contain the (-NH2OH) radical.Fish Proteins: Proteins obtained from species of fish (FISHES).Isomerism: The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Retinal Photoreceptor Cell Outer Segment: The light sensitive outer portion of a retinal rod or a cone photoreceptor cell. The outer segment contains a stack of disk membranes laden with photoreceptive pigments (RETINAL PIGMENTS). The outer segment is connected to the inner segment by a PHOTORECEPTOR CONNECTING CILIUM.Urodela: An order of the Amphibia class which includes salamanders and newts. They are characterized by usually having slim bodies and tails, four limbs of about equal size (except in Sirenidae), and a reduction in skull bones.Fluorescent Antibody Technique, Indirect: A form of fluorescent antibody technique commonly used to detect serum antibodies and immune complexes in tissues and microorganisms in specimens from patients with infectious diseases. The technique involves formation of an antigen-antibody complex which is labeled with fluorescein-conjugated anti-immunoglobulin antibody. (From Bennington, Saunders Dictionary & Encyclopedia of Laboratory Medicine and Technology, 1984)Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Lizards3',5'-Cyclic-GMP Phosphodiesterases: Enzymes that catalyze the hydrolysis of cyclic GMP to yield guanosine-5'-phosphate.Invertebrates: Animals that have no spinal column.Kinetics: The rate dynamics in chemical or physical systems.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Animals, Genetically Modified: ANIMALS whose GENOME has been altered by GENETIC ENGINEERING, or their offspring.Ambystoma: A genus of the Ambystomatidae family. The best known species are the axolotl AMBYSTOMA MEXICANUM and the closely related tiger salamander Ambystoma tigrinum. They may retain gills and remain aquatic without developing all of the adult characteristics. However, under proper changes in the environment they metamorphose.GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Vertebrates: Animals having a vertebral column, members of the phylum Chordata, subphylum Craniata comprising mammals, birds, reptiles, amphibians, and fishes.cis-trans-Isomerases: Enzymes that catalyze the rearrangement of geometry about double bonds. EC 5.2.Archaeal Proteins: Proteins found in any species of archaeon.Norisoprenoids: Thirteen-carbon butene cyclohexene degradation products formed by the cleavage of CAROTENOIDS. They contribute to the flavor of some FRUIT. Ionone should not be confused with the similarly named ionol.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Arrestin: A 48-Kd protein of the outer segment of the retinal rods and a component of the phototransduction cascade. Arrestin quenches G-protein activation by binding to phosphorylated photolyzed rhodopsin. Arrestin causes experimental autoimmune uveitis when injected into laboratory animals.Color: The visually perceived property of objects created by absorption or reflection of specific wavelengths of light.Arthropods: Members of the phylum Arthropoda, composed of organisms having a hard, jointed exoskeleton and paired jointed legs. It includes the class INSECTS and the subclass ARACHNIDA, many species of which are important medically as parasites or as vectors of organisms capable of causing disease in man.Thyroid Hormone Receptors beta: High affinity receptors for THYROID HORMONES, especially TRIIODOTHYRONINE. These receptors are usually found in the nucleus where they regulate DNA transcription. They are encoded by the THRB gene (also known as NR1A2, THRB1, or ERBA2 gene) as several isoforms produced by alternative splicing. Mutations in the THRB gene cause THYROID HORMONE RESISTANCE SYNDROME.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Halobacterium: A genus of HALOBACTERIACEAE whose growth requires a high concentration of salt. Binary fission is by constriction.Decapodiformes: A superorder of CEPHALOPODS comprised of squid, cuttlefish, and their relatives. Their distinguishing feature is the modification of their fourth pair of arms into tentacles, resulting in 10 limbs.Retinoids: A group of tetraterpenes, with four terpene units joined head-to-tail. Biologically active members of this class are used clinically in the treatment of severe cystic ACNE; PSORIASIS; and other disorders of keratinization.Photic Stimulation: Investigative technique commonly used during ELECTROENCEPHALOGRAPHY in which a series of bright light flashes or visual patterns are used to elicit brain activity.Halobacteriaceae: A family of extremely halophilic archaea found in environments with high salt concentrations, such as salt lakes, evaporated brines, or salted fish. Halobacteriaceae are either obligate aerobes or facultative anaerobes and are divided into at least twenty-six genera including: HALOARCULA; HALOBACTERIUM; HALOCOCCUS; HALOFERAX; HALORUBRUM; NATRONOBACTERIUM; and NATRONOCOCCUS.Gene Duplication: Processes occurring in various organisms by which new genes are copied. Gene duplication may result in a MULTIGENE FAMILY; supergenes or PSEUDOGENES.In Situ Hybridization: A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.Receptors, G-Protein-Coupled: The largest family of cell surface receptors involved in SIGNAL TRANSDUCTION. They share a common structure and signal through HETEROTRIMERIC G-PROTEINS.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Ranidae: The family of true frogs of the order Anura. The family occurs worldwide except in Antarctica.
  • This greatly increases the membrane surface area, and thus the amount of opsin, in these light-detecting cells. (encyclopedia.com)
  • Nir I, Papermaster DS (1986) Immunocytochemical localization of opsin in the inner segment and ciliary plasma membrane of photoreceptors in retinas of rds mutant mice. (springer.com)
  • To test this hypothesis, we used deep mutational scanning to compare the effects of 808 missense mutations on the plasma membrane expression of rhodopsin in HEK293T cells. (sciencemag.org)
  • Atomistic molecular dynamics simulations of wild type and QUAD opsins combined with continuum modeling revealed that the tryptophan substitutions lower the energetically unfavorable residual hydrophobic mismatch between TM4 and the membrane, reducing the drive of QUAD opsin to dimerize. (deepdyve.com)
  • mismatch between TM4 and the membrane, reducing the drive of QUAD opsin to dimerize. (deepdyve.com)
  • Combined quantum mechanical and molecular mechanical (QM/MM) calculations and molecular dynamics simulations of bacteriorhodopsin (bR) in the membrane matrix have been carried out to determine the factors that make significant contributions to the opsin shift. (semanticscholar.org)
  • Rhodopsin self-associates in the plasma membrane. (springer.com)
  • To quantify rhodopsin interactions, I will outline the theory and methodology of a specialized time-resolved fluorescence spectroscopy for measuring membrane protein-protein interactions called pulsed-interleaved excitation fluorescence cross-correlation spectroscopy (PIE-FCCS). (springer.com)
  • The strength of this technique is its ability to quantify rhodopsin interactions in situ (i.e., a live cell plasma membrane). (springer.com)
  • When wild-type opsin and G188R opsin were coexpressed in cells, properly folded wild-type opsin did not aggregate with G188R opsin and was trafficked normally to the cell membrane. (antibodies-online.com)
  • In developing Drosophila photoreceptors, rhodopsin is trafficked to the rhabdomere, a specialized domain within the apical membrane surface. (biologists.org)
  • These results support the idea that the rhodopsin-containing photoreceptors of P. melanoleucus are the products of evolutionary transmutation from rod ancestors, and suggest that this phenomenon may be widespread in colubrid snakes. (biologists.org)
  • There is great diversity among butterfly species, in the wavelength for peak sensitivity (λ max ) of rhodopsins found in photoreceptors of the compound eyes. (biologists.org)
  • Nir I, Papermaster DS (1989) Immunocytochemical localization of opsin in degenerating photoreceptors of RCS rats and rd and rds mice. (springer.com)
  • Immature rhodopsin, which is indicative of defective rhodopsin transport, accumulated in Drosophila photoreceptors that expressed dominant-negative Rab11 N124I ( Satoh, 1998 ). (biologists.org)
  • TMT-Opsin subclasses are specifically expressed not only in hypothalamic and thalamic deep brain photoreceptors, but also in interneurons and motorneurons with no known photoreceptive function, such as the typeXIV interneurons of the fish optic tectum. (nih.gov)
  • The blot was probed with a 1:2,000 dilution of antisera (CERN 886) raised against bovine rhodopsin and detected by enhanced chemiluminescence. (pnas.org)
  • To lay the molecular basis driving the evolutionary transition from the all- trans to the 11- cis chromophore, multiconfigurational quantum chemistry is used to compare the isomerization mechanisms of the sensory rhodopsin from the cyanobacterium Anabaena PCC 7120 (ASR) and of the bovine rhodopsin (Rh). (pnas.org)
  • Recombinant fragment corresponding to Bovine Rhodopsin (N terminal). (abcam.com)
  • In the present work, the successful crystallization of native opsin from bovine retinal rod cells and determination of the protein structure to 2.9 Å resolution is presented. (hu-berlin.de)
  • We show that, by using light-responsive computer models of a eubacterial sensory rhodopsin and of a vertebrate visual rhodopsin, it is possible to identify a distinctive electronic character of the 11- cis chromophore that could have become an effective target for natural selection. (pnas.org)
  • It is found that, despite their evolutionary distance, these eubacterial and vertebrate rhodopsins start to isomerize via distinct implementations of the same bicycle-pedal mechanism originally proposed by Warshel [Warshel A (1976) Nature 260:678- (pnas.org)
  • We find that the vertebrate medium wavelength cone opsin (MW-opsin) overcomes these limitations and supports vision in dim light. (nih.gov)
  • The expression of these genes, the differential expression of opsin based on light exposure and the unique morphological features at the distal portion of the tube foot strongly support the hypothesis that in addition to previously identified functional roles of tube feet they are also photosensory organs that detect and respond to changes in the underwater light field. (royalsocietypublishing.org)
  • Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. (nih.gov)
  • GTF2IRD1 binds to enhancer and promoter regions in the mouse rhodopsin, M- and S-opsin genes, but regulates their expression differentially. (jove.com)
  • Menon, Anant 2017-12-01 00:00:00 The G protein-coupled receptor opsin is a phospholipid scramblase that facilitates rapid transbilayer phospholipid exchange in liposomes. (deepdyve.com)
  • Microbial and animal rhodopsins share several striking structural features including a seven α-helix fold and a highly conserved active-site lysine in the seventh helix. (pnas.org)
  • In this paper we address the question of why the sequence of animal rhodopsins, featuring an 11- cis chromophore, could have diverged from a microbial ancestor incorporating the more stable all- trans chromophore. (pnas.org)
  • The functions of microbial and animal rhodopsins are triggered by the isomerization of their all- trans and 11- cis retinal chromophores, respectively. (pnas.org)
  • It is argued that the optimization of the electronic properties of the chromophore, which affects the photoisomerization efficiency and the thermal isomerization barrier, provided a key factor for the emergence of the striking amino acid sequence divergence observed between the microbial and animal rhodopsins. (pnas.org)
  • Neuroscientists initially used naturally occurring microbial opsins and later mutated versions of these opsins to alter the flux of ions across membranes to drive cell activity. (dovepress.com)
  • 14 , 15 Microbial opsins have been incorporated in combination with numerous mouse transgenic technologies and viral constructs. (dovepress.com)
  • Over the past 10 years, the development and convergence of microbial opsin engineering, modular genetic methods for cell-type targeting and optical strategies for guiding light through tissue have enabled versatile optical control of defined cells in living systems, defining modern optogenetics. (nih.gov)
  • In the early 1970s, researchers identified bacteriorhodopsin as a light-activated ion pump and the first of what was to become an expanding palette of so-called microbial opsins. (genengnews.com)
  • The advantage of microbial opsins is that they are single-component systems-they combine light sensitivity and effector function in a single protein. (genengnews.com)
  • Long Wavelength Sensitive ( OPN1LW ) Opsin - λ max of 560 nm, in the yellow-green region of the electromagnetic spectrum. (wikipedia.org)
  • This helix runs approximately parallel to the cytoplasmic surface and is involved in Gtγ binding , as well as the modulation of rhodopsin-transducin interactions and rhodopsin-phospholipid interactions . (proteopedia.org)
  • RA was shown to interact with the UV-cone opsin, demonstrated by its ability to effect ligand-dependent activation of transducin by UV-cone opsin. (molvis.org)
  • Sensory rhodopsin II (rainbow colored) embedded in a lipid bilayer (heads red and tails blue) with Transducin below it. (bionity.com)
  • It interacts with photo-activated phosphorylated rhodopsin, inhibiting or 'arresting' its ability to interact with transducin [ PMID: 15335861 ]. (ebi.ac.uk)
  • We recently found the expression and maturation of rhodopsin are limited by the hydrophobicity of its seventh transmembrane domain (TM7), which contains polar residues that are essential for function. (sciencemag.org)