Structural and functional aspects of RGD-containing protein antagonists of glycoprotein IIb-IIIa.
In the past few years, knowledge of the structure and function of RGD-containing protein antagonists of the platelet fibrinogen receptor glycoprotein IIb-IIIa has advanced rapidly. The RGD sequence is found at the apex of extended, solvent accessible, and conformationally flexible loops in proteins of vastly different structural frameworks. Conformation of the RGD epitope and the immediate surrounding sequence are critical factors affecting potency and selectivity as integrin antagonists. The RGD sequence has recently been introduced into a number of protein and peptide scaffolds.
Lazarus
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Department of Protein Engineering Genentech Inc., South San Francisco, California 94080.
McDowell
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D000595:Amino Acid Sequence; D000818:Animals; D001709:Biotechnology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology*; D010980:Platelet Membrane Glycoproteins / Q000037:antagonists & inhibitors*; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology
D009842:Oligopeptides; D010980:Platelet Membrane Glycoproteins; D011506:Proteins; C047981:arginyl-glycyl-aspartic acid