Localization of an Arg-Gly-Asp Recognition Site Within an Integrin Adhesion Receptor

• DOI: 10.1126/science.3262922
• Publication Date: 2006-10-05T21:21:15Z
• Authors: Stanley E. D'Souza; Mark H. Ginsberg; Timothy A. Burke; Stephen C.-T. Lam; Edward F. Plow
• Keywords: Blood Platelets; 0301 basic medicine; Integrins; Binding Sites; Membrane Glycoproteins; Receptors, Peptide; Molecular Sequence Data; Platelet Membrane Glycoproteins; 03 medical and health sciences; Humans; Amino Acid Sequence; Receptors, Immunologic; Protein Binding

Many adhesive interactions are mediated by Arg-Gly-Asp (RGD) sequences within adhesive proteins. Such RGD sequences are frequently recognized by structurally related heterodimers that are members of the integrin family of adhesion receptors. A region was found in the platelet RGD receptor, gpIIb/IIIa, to which an RGD peptide becomes chemically cross-linked. This region corresponds to residues 109 to 171 of gpIIIa. This segment is conserved among the β subunits of the integrins (76 percent identity of sequence), indicating that it may play a role in the adhesive functions of this family of receptors.