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

Abstract

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.

Keywords

IntegrinReceptorAdhesionChemistryPeptide sequenceSequence (biology)PeptideCell adhesionCell biologyBiochemistryBiologyGene

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Publication Info

Year: 1988
Type: article
Volume: 242
Issue: 4875
Pages: 91-93
Citations: 397
Access: Closed

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APA Style

                            
                                
                                    Stanley E. D’Souza, 
                                
                                    Mark H. Ginsberg, 
                                
                                    Timothy Burke
                                
                                et al.
                            
                            (1988). 
                            Localization of an Arg-Gly-Asp Recognition Site Within an Integrin Adhesion Receptor. 
                            Science
                            , 242
                            (4875)
                            , 91-93.
                            https://doi.org/10.1126/science.3262922
                        

Identifiers

DOI: 10.1126/science.3262922