Back to your search result

Description

Integrin aV (UniProt: P06756, also known as Vitronectin receptor, Vitronectin receptor subunit alpha, CD51) is encoded by the ITGAV (also known as MSK8, VNRA, VNTR) gene (Gene ID: 3685) in human. Integrins are heterodimeric integral membrane proteins composed of an a subunit and a b subunit that function in cell surface adhesion and signaling. They contain a large extracellular domain responsible for ligand binding, a single transmembrane domain, and a cytoplasmic domain. The exact combination of various a- and b-subunits dictates the binding specificity of integrins to different ECM components. Although both subunits are required for adhesion, the binding specificity primarily depends on the extracellular portion of the a-subunit. The structural and functional diversity of the integrin family is based upon the pairing abilities of the individual a and b subunits. Integrins are not constitutively active and their activation from a low ligand-binding affinity state to high ligand-binding affinity state requires conformational change that can originate from either from their cytoplasmic or extracellular interactions. The recognition site for most integrins that bind the ECM consists of an RGD (arginine-glycine-aspartic acid) sequence. Integrin aV is a single-pass membrane glycoprotein that is synthesized with a signal peptide (aa 1-30), which is subsequently cleaved off to generate the mature form. The mature form contains an extracellular domain (aa 31-992), a transmembrane domain (aa 993-1016), and a cytoplasmic domain (aa 1017-1048). The a-subunit is composed of a heavy (aa 31-889) and a light (aa 891-1048) chain linked by a disulfide bond. Integrin aV can associate with b-1, b-3, b -5, b-6, or b-8 in a non-covalent manner. (Ref.: Cheresh, DA. (1987). Proc. Natl. Acad. Sci. USA. 84(18), 6471-6475).