Integrin alpha-V beta-3 complex (αVβ3 (or αvβ3))

Integrin alpha-V beta-3 complex is a heterodimeric transmembrane receptor from the integrin superfamily, composed of alpha-V (CD51) and beta-3 (CD61) subunits. This receptor mediates cell adhesion to the extracellular matrix via recognition of the Arg-Gly-Asp (RGD) motif present in ligands such as vitronectin, fibronectin, and osteopontin. The αVβ3 integrin is expressed on various cell types, including endothelial cells, osteoclasts, and some tumor cells. Through both "inside-out" and "outside-in" signaling, it regulates processes such as cell migration, survival, proliferation, and angiogenesis. Its dysregulation is implicated in the progression of cancer (tumor growth, invasion, metastasis, angiogenesis), cardiovascular diseases, inflammatory conditions, and disorders relating to bone remodeling. The structure of the integrin αVβ3 ectodomain reveals a bent conformation and an RGD-binding site formed by the αV β-propeller and β3 βI domains, with dynamic conformational changes being critical for activation and signaling. Due to its role in disease, αVβ3 is a validated therapeutic target, with several antagonists developed for oncology, cardiovascular, and musculoskeletal indications[1][2][5][6][7].

Other names

Integrin αVβ3αvβ3 integrinVitronectin receptorCD51/CD61

Competitive antagonism of RGD ligand binding (e.g., by mimicking the RGD motif) Induction of apoptosis (e.g., by non-RGD site binding, as with ProAgio) Inhibition of integrin-mediated signal transduction Disruption of cell-matrix interactions and angiogenesis