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Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist
M Adler1, R A Lazarus, M S Dennis
1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Science (New York, N.Y.)
|July 26, 1991
Abstract:
The structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein.