Research Articles

Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist

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Science  26 Jul 1991:
Vol. 253, Issue 5018, pp. 445-448
DOI: 10.1126/science.1862345


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.

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