SOLUTION STRUCTURE OF KISTRIN, A POTENT PLATELET-AGGREGATION INHIBITOR AND GP-IIB-IIIA ANTAGONIST
SOLUTION STRUCTURE OF KISTRIN, A POTENT PLATELET-AGGREGATION INHIBITOR AND GP-IIB-IIIA ANTAGONIST
复制标题
DOI:
10.1126/science.1862345
复制
发表时间:
1991-07-26
期刊:
影响因子:
56.9
通讯作者:
WAGNER, G
中科院分区:
文献类型:
--
作者:
ADLER, M;LAZARUS, RA;WAGNER, G
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.