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Science 7 October 1988:
Vol. 242. no. 4875, pp. 91 - 93
DOI: 10.1126/science.3262922
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Articles

Science, Vol 242, Issue 4875, 91-93
Copyright © 1988 by American Association for the Advancement of Science

articles

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

SE D'Souza, MH Ginsberg, TA Burke, SC Lam, and EF Plow

Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.

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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Integrin alpha subunit mRNAs are differentially expressed in early Xenopus embryos.
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   Abstract »    PDF »
Ligand Binding to Integrins: Dynamic Regulation and Common Mechanisms.
M.H. Ginsberg, T.E. O'Toole, J.C. Loftus, and E.F. Plow (1992)
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   Abstract »    PDF »
A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation.
J. Loftus, T. O'Toole, E. Plow, A Glass, A. Frelinger 3rd, and M. Ginsberg (1990)
Science 249, 915-918
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Structure and Regulation of the Leukocyte Adhesion Receptor LFA-1 and Its Counterreceptors, ICAM-1 and ICAM-2.
M.L. Dustin, J. Garcia-Aguilar, M.L. Hibbs, R.S. Larson, S.A. Stacker, D.E. Staunton, A.J. Wardlaw, and T.A. Springer (1989)
Cold Spring Harb Symp Quant Biol 54, 753-765
   Abstract »    PDF »
Molecular Basis of Ligand Recognition by Integrin alpha 5beta 1. II. SPECIFICITY OF Arg-Gly-Asp BINDING IS DETERMINED BY Trp157 OF THE alpha SUBUNIT.
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J. Biol. Chem. 275, 20337-20345
   Abstract »    Full Text »    PDF »
Molecular Basis of Ligand Recognition by Integrin alpha 5beta 1. I. SPECIFICITY OF LIGAND BINDING IS DETERMINED BY AMINO ACID SEQUENCES IN THE SECOND AND THIRD NH2-TERMINAL REPEATS OF THE alpha SUBUNIT.
A. P. Mould, J. A. Askari, and M. J. Humphries (2000)
J. Biol. Chem. 275, 20324-20336
   Abstract »    Full Text »    PDF »
Structure-Function of the Putative I-domain within the Integrin beta 2 Subunit.
Y.-M. Xiong and L. Zhang (2001)
J. Biol. Chem. 276, 19340-19349
   Abstract »    Full Text »    PDF »
RGD-containing Peptides Inhibit Fibrinogen Binding to Platelet alpha IIbbeta 3 by Inducing an Allosteric Change in the Amino-terminal Portion of alpha IIb.
R. B. Basani, G. D'Andrea, N. Mitra, G. Vilaire, M. Richberg, M. A. Kowalska, J. S. Bennett, and M. Poncz (2001)
J. Biol. Chem. 276, 13975-13981
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)