TailsHeterodimersExtracellular matrixFocal-adhesion moleculeTensinReceptorsConformationHomologyPleckstrinAntibodyInteractionsTyrosine kinaseMolecularProtein kinasesActin cytoskeletonHydrogenResiduesProteins containPeptideLigandsTranscriptionInteractionSubunitsRegulationFamilySequenceFunctionCapped by a C-terminalFoundSimilarSiteNuclearActivityStructure
Tails4
- The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif. (wikipedia.org)
- The ECM proteins bind to the extracellular domains of integrin heterodimers, whereas the actin stress fibers link to integrin cytoplasmic tails via large molecular complexes. (rupress.org)
- Each integrin heterodimer consists of an alpha (α) and a beta (β) subunit associated by noncovalent interactions forming an extracellular ligand-binding head, two multi-domain `legs', two single-pas s transmembrane helices and two short cytoplasmic tails. (mechanobio.info)
- The chromo-domain binds histone H3 tails methylated on lysine 9. (cipsm.de)
Heterodimers1
- The integrin family of proteins consists of alpha and beta subtypes, which form transmembrane heterodimers. (mechanobio.info)
Extracellular matrix3
- Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). (wikipedia.org)
- Integrins are proteins that function mechanically, by attaching the cell cytoskeleton to the extracellular matrix (ECM), and biochemically, by sensing whether adhesion has occurred. (mechanobio.info)
- Integrin allosteric changes, clustering, and trafficking cooperate to regulate cell adhesion and motility on extracellular matrix proteins via mechanisms that are partly defined. (life-science-alliance.org)
Focal-adhesion molecule1
- The tensin family member cten (C-terminal tensin like) is an Src homology 2 (SH2) and phosphotyrosine binding domain-containing focal adhesion molecule that may function as a tumor suppressor. (rupress.org)
Tensin5
- The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. (wikipedia.org)
- Human tensin has actin-binding sites, an SH2 (Pfam PF00017) domain and a region similar to the tumour suppressor PTEN. (wikipedia.org)
- The phosphotyrosine-binding domain of insulin receptor substrate-1 is not related to the phosphotyrosine-binding domain of tensin. (wikipedia.org)
- Tensin is a gene family with four members (tensin1, tensin2, tensin3, and cten), and their encoding proteins are localized to the cytoplasmic side of focal adhesions. (rupress.org)
- By exploiting four monoclonal antibodies recognizing distinct conformational epitopes, we show that in endothelial cells (ECs), the extracellular βI domain, but not the hybrid or I-EGF2 domain of active β1 integrins, promotes their FAK-regulated clustering into tensin 1-containing fibrillar adhesions and impairs their endocytosis. (life-science-alliance.org)
Receptors3
- Integrins function as adhesion receptors for extracellular ligands and transduce biochemical signals into the cell, through downstream effector proteins. (mechanobio.info)
- The 3' replication has freely activated by RNase Z surface, a mature binding in receptors( reviewed in Maraia and Lamichhane 2011). (evakoch.com)
- Siglecs are a family of sialic acid-binding immunoglobulin-like receptors predominantly expressed on cells of immune system to regulate their functions through recognizing their glycan ligands [ 5 ]. (biomedcentral.com)
Conformation1
- Here we report the selection of camelid-derived single-domain antibodies (nanobodies) that modulate the conformation and spectral properties of the green fluorescent protein (GFP). (cipsm.de)
Homology3
- Insulin receptor substrate-1 proteins contain both a pleckstrin homology domain and a phosphotyrosine binding (PTB) domain. (wikipedia.org)
- Pleckstrin homology domain. (embl.de)
- Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of proteins. (embl.de)
Pleckstrin2
Antibody1
- This Antibody was verified by Cell treatment to ensure that the antibody binds to the antigen stated. (thermofisher.cn)
Interactions3
- Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways. (embl.de)
- The dynamic regulation of the physical interactions of integrins with the ECM is necessary for physiological function, and it is disrupted in pathological settings ( Seguin et al, 2015 ). (life-science-alliance.org)
- Syk binds to the receptor assemblies through interactions of its pair of SH2 domains with ITAM motives of the receptor, which have been phosphorylated by Src-family kinases. (thermofisher.cn)
Tyrosine kinase2
- Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. (embl.de)
- Spleen tyrosine kinase (SYK), along with ZAP70, are cytoplasmic tyrosine kinases that are viewed as potential druge targets for allergic disorders and autoimmune diseases. (thermofisher.cn)
Molecular1
- In molecular biology, Phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine. (wikipedia.org)
Protein kinases1
- Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family. (embl.de)
Actin cytoskeleton1
- Focal adhesions are integrin-mediated cell matrix junctions connecting the ECM to the actin cytoskeleton. (rupress.org)
Hydrogen1
- Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac-LYASSNPApY-NH2 peptide in the juxtamembrane region of the insulin receptor. (wikipedia.org)
Residues2
Proteins contain1
Peptide1
Ligands1
- Siglec-E, a mouse orthologue of human Siglec-9, is a sialic acid binding lectin predominantly expressed on the surface of myeloid cells to transduce inhibitory signal via recruitment of SH2-domain containing protein tyrosine phosphatase SHP-1/2 upon binding to its sialoglycan ligands. (biomedcentral.com)
Transcription1
- TATA-box binding protein is not required for RNA Polymerase II transcription in mouse embryonic stem cells. (elifesciences.org)
Interaction3
- The PTB domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. (wikipedia.org)
- We report that cten binds to another tumor suppressor, deleted in liver cancer 1 (DLC-1), and the SH2 domain of cten is responsible for the interaction. (rupress.org)
- Unexpectedly, the interaction between DLC-1 and the cten SH2 domain is independent of tyrosine phosphorylation of DLC-1. (rupress.org)
Subunits1
- The communication in subunit: enabling lymphoid GT-domains preventing membrane as a subunits addition: A ATM identified to the Faculty of Graduate Studies and Research in isolated pore of the heterotrimers for the use of Master of Nursing. (evakoch.com)
Regulation2
Family2
- The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. (embl.de)
- The Aβ domain is unique to the APP protein, though the family shares several other conserved domains such as the E1 and E2 domains in the extracellular sequence. (biomedcentral.com)
Sequence1
- The β subunit comprises of 4 cysteine-rich epidermal growth factor (EGF) repeats, a hybrid domain (split in sequence), an I-like domain (βI) and a plexin-sempahorin-integrin (PSI) domain. (mechanobio.info)
Function2
- The RPA gene is the structural excretion loss-of-function, However Binding it from the corresponding growth( De Laat et al. (evakoch.com)
- Modulation of integrin function is required in many physiological and pathological settings, such as angiogenesis and cancer. (life-science-alliance.org)
Capped by a C-terminal1
- The PTB domain has a compact, 7-stranded beta-sandwich structure, capped by a C-terminal helix. (wikipedia.org)
Found2
Similar1
- Similar to αI, the contains βI domain contains a MIDAS site for ligand binding and additional regulatory site "adjacent to MIDAS" or ADMIDAS, inhibited by Ca2+ and activated by Mn2+ [3] for ligand binding. (mechanobio.info)
Site1
- Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. (embl.de)
Nuclear1
Activity1
- These results provide a novel mechanism whereby the SH2 domain of cten-mediated focal adhesion localization of DLC-1 plays an essential role in its tumor suppression activity. (rupress.org)
Structure1
- Middle: The globular structure formed by protein domains. (mechanobio.info)