Literature DB >> 3262922

Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor.

S E D'Souza1, M H Ginsberg, T A Burke, S C Lam, E F Plow.   

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 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.

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Year:  1988        PMID： 3262922     DOI： 10.1126/science.3262922

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  62 in total

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