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Protein SubunitsModels, MolecularDisulfidesProtein Structure, QuaternaryRibosome Subunits, Large, BacterialDimerizationProtein ConformationBinding SitesCysteineCrystallography, X-RayMacromolecular SubstancesRibosome Subunits, Small, BacterialAmino Acid SequenceMolecular Sequence DataMutagenesis, Site-DirectedAllosteric RegulationProtein Structure, TertiaryProtein Structure, SecondaryProtein BindingEnzyme StabilityEscherichia coliLigand-Gated Ion ChannelsProtein MultimerizationCryoelectron MicroscopyAllosteric SiteReducing AgentsKineticsMutationCross-Linking ReagentsDithiothreitolAmino Acid SubstitutionAspartate CarbamoyltransferaseTryptophan SynthaseIon Channel GatingSulfhydryl ReagentsModels, StructuralRecombinant ProteinsPeptide Elongation Factor GStructure-Activity RelationshipBacterial ProteinsRibosomesCatalysisProtein Interaction Domains and MotifsProtein DenaturationRibosemonophosphatesThermus thermophilusPhenanthrolinesAspartic AcidShaker Superfamily of Potassium ChannelsProtein FoldingCatalytic DomainPyroglutamyl-Peptidase ISequence Homology, Amino AcidCyclic Nucleotide-Gated Cation ChannelsEscherichia coli ProteinsMolecular Docking SimulationCircular DichroismXenopus laevisHydrogen BondingHydrogen-Ion ConcentrationAdenosine TriphosphateSulfhydryl CompoundsThermodynamicsRNA, TransferModels, ChemicalOxidation-ReductionProtein StabilitySaltsBiopolymersPyrococcus furiosusEthylmaleimideBase SequenceProtein EngineeringRibosomal ProteinsMolecular ConformationFluorescence Resonance Energy TransferLigandsElectrophoresis, Polyacrylamide GelMutation, MissenseRNA, Ribosomal, 23SOocytesX-Ray DiffractionHydrolysisNucleotides, CyclicMutagenesisStatic ElectricityRNA, BacterialSubstrate SpecificityVirus AssemblyAcetylcholinesteraseCrystallographyHot TemperatureAlanineTorpedoXenopusProtein BiosynthesisProton-Translocating ATPasesZincDithionitrobenzoic AcidSpectrometry, Fluorescence
DisulfideInteractionsStabilizeRibosomeBondCommunicationBetaCaseContactsSiteDomain
Disulfide2
  • Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion. (rush.edu)
  • The reduced thioredoxin cleaves an intersubunit disulfide bond to activate the redox switch and reactivate the enzyme. (prospecbio.com)
Interactions3
  • intersubunit interactions leading to changes in oligomeric structure and exposure of specific regions may modulate their functioning. (nih.gov)
  • Intersubunit interactions associated with tyr42alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin. (expasy.org)
  • When fully liganded with carbon monoxide, Hb zeta(2)beta(s)(2) displays a central water cavity, a zeta 1-beta(s)2 (or zeta 2-beta(s)1) interface, intersubunit salt-bridge/hydrogen-bond interactions, C-terminal beta His146 salt-bridge interactions, and a beta-cleft, that are highly unusual for a relaxed hemoglobin structure and are more typical of a tense conformation. (janelia.org)
Stabilize1
Ribosome4
  • Ribosomal protein S15 is of particular interest because it binds primarily to 16S rRNA and is required for assembly of the small subunit and for intersubunit association, thus representing a key element in the assembly of a whole ribosome. (unboundmedicine.com)
  • Knockout of KsgA, which methylates two adjacent adenosines at positions 1518 and 1519 of 16S rRNA in the intersubunit bridge of the ribosome, attenuated the S. aureus killing ability against silkworms. (elsevierpure.com)
  • Three-dimensional Cryo-electron microscopic (Cryo-EM) reconstructions reveal that, like pY, PSRP1 binds within the intersubunit space of the 70S ribosome, at a site overlapping the positions of mRNA and A- and P-site tRNAs. (cipsm.de)
  • PSRP1 induces conformational changes within ribosomal components that comprise several intersubunit bridges, including bridge B2a, thereby stabilizes the ribosome against dissociation.Wefind that the presence ofPSRP1/pYlowers the binding of tRNA to the ribosome. (cipsm.de)
Bond1
  • Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond. (fortlewis.edu)
Communication2
  • This intersubunit communication pushes the Rag GTPases into either of two stable configurations, which represent active "on" or "off" states that interconvert via transient intermediates. (broadinstitute.org)
  • There are two main mechanisms for intersubunit communication. (wikipedia.org)
Beta1
  • From the differences in intersubunit contacts among beta(4), gamma(4), and delta(4), we formed a hypothesis regarding the possible tetramerization pathway of delta(4). (rcsb.org)
Case1
  • In this case the intersubunit distance restraints will be derived automatically i.e. the units will be oriented similarly as in the template complex and 'see' each other. (salilab.org)
Contacts2
  • Using crosslinking and two- electrode voltage clamp in Xenopus oocytes , we identified several pairs of functional intersubunit contacts where mouse ENaC activity was modulated by inducing or breaking a disulfide bond between introduced Cys residues. (bvsalud.org)
  • Role of Interdomain and Intersubunit Contacts for NMDA Receptor Function. (tu-darmstadt.de)
Site3
  • Here, experimental evidence for carboxylate binding to GLIC is provided by solving its X-ray structures with a series of monocarboxylate and dicarboxylate derivatives, and two carboxylate-binding sites are described: (i) the `intersubunit' site that partially overlaps the canonical pLGIC orthosteric site and (ii) the `intrasubunit' vestibular site, which is only occupied by a subset of the described derivatives. (rcsb.org)
  • While the intersubunit site is widely conserved in all pLGICs, the intrasubunit site is only conserved in cationic eukaryotic pLGICs. (rcsb.org)
  • Detailed kinetic, biophysical and structural evidence reveals that BRD4592 is an allosteric, mixed-type inhibitor, which binds specifically to a novel site within the intersubunit channel, at the TrpA-TrpB interface. (nih.gov)
Domain1
  • The data show structural equivalence between heat-induced and ex vivo polymers and that the intersubunit linkage is best explained by a carboxyl-terminal domain swap between molecules of α1-antitrypsin. (kcl.ac.uk)