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The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit.

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Smith, J W, Cheresh, D A·1988·Journal of Biological Chemistry

Abstract

We have employed photoaffinity cross-linking to examine RGD recognition by the human placental vitronectin receptor. The peptide GRGDSPK was coupled to a thiol-cleavable radioiodinatable aryl azide (sulfosuccinimidyl 2-(p-azido-salicylamido)-1,3'-dithiopropionate. When 125I-sulfosuccinimidyl 2-(p-azido-salicylamido)-1,3'-dithiopropionate-GRGDSPK was cross-linked to the vitronectin receptor in solution, 80% of the label was associated with the beta subunit. Cross-linking to both subunits of the receptor was highly specific and dependent upon the presence of divalent cations. Ca2+ and Mg2+ promoted RGD recognition by the receptor; however, the effects of each divalent cation were kinetically distinct. We have also identified and determined the amino acid sequence of chymotryptic and V8 protease-generated peptides of the beta subunit that were radiolabeled as a result of cross-linking. The results of these studies demonstrate that amino acid residues 61-203 are proximal to the RGD binding domain of the vitronectin receptor.

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Metadata

Authors
Smith, J. W., & Cheresh, D. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1988-12
Volume
263
Issue
35
Pages
18726-18731
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1594881395
Cited by
234
References
0
FWCI
7.60
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit. https://app.cochat.ai/papers/10.1016/s0021-9258(18)37343-5
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Smith, J. W., & Cheresh, D. A. (1988). The Arg-Gly-Asp binding domain of the vitronectin receptor. Photoaffinity cross-linking implicates amino acid residues 61-203 of the beta subunit. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)37343-5

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