Localization of an Arg-Gly-Asp Recognition Site Within an Integrin Adhesion Receptor
- 7 October 1988
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 242 (4875), 91-93
- https://doi.org/10.1126/science.3262922
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.This publication has 31 references indexed in Scilit:
- New Perspectives in Cell Adhesion: RGD and IntegrinsScience, 1987
- Amino acid sequence of the human fibronectin receptor.The Journal of cell biology, 1987
- Competition for related but nonidentical binding sites on the glycoprotein IIb-IIIa complex by peptides derived from platelet adhesive proteinsCell, 1987
- Cloning of the $beta; subunit of the leukocyte adhesion proteins: Homology to an extracellular matrix receptor defines a novel supergene familyCell, 1987
- Integrins: A family of cell surface receptorsCell, 1987
- LEUKOCYTE ADHESION DEFICIENCY: An Inherited Defect in the Mac-1, LFA-1, and p150,95 GlycoproteinsAnnual Review of Medicine, 1987
- Platelet Membrane Glycoprotein IIb/IIIa: Member of a Family of Arg-Gly-Asp—Specific Adhesion ReceptorsScience, 1986
- Arg-Gly-Asp: A versatile cell recognition signalCell, 1986
- Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule.The Journal of cell biology, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970