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

• Published in: Science (American Association for the Advancement of Science) 1988-10, Vol.242 (4875), p.91-93
• Main Authors: D'Souza, Stanley E., Ginsberg, Mark H., Burke, Timothy A., Stephen C.-T. Lam, Plow, Edward F.
• Format: Article
• Language: English
• Subjects: Adhesion; Adhesives; Amino Acid Sequence; Amino acids; Binding Sites; Biological and medical sciences; Blood; Blood Platelets - immunology; Cell adhesion; Cell interactions, adhesion; Cell receptors; Fundamental and applied biological sciences. Psychology; Gels; Humans; Immunity (Disease); integrin; Integrins; Ligands; Medical research; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Molecular and cellular biology; Molecular Sequence Data; Platelet Membrane Glycoproteins - genetics; Platelet Membrane Glycoproteins - metabolism; Platelets; Plows; Protein Binding; Radioactive decay; Receptors; Receptors, Immunologic - metabolism; Receptors, Peptide
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.3262922

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 $\beta $ 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.