CYSTEINE PAIRING IN THE GLYCOPROTEIN-IIBIIIA ANTAGONIST KISTRIN USING NMR, CHEMICAL-ANALYSIS, AND STRUCTURE CALCULATIONS

被引：41

作者：

ADLER, M

CARTER, P

LAZARUS, RA

WAGNER, G

机构：

[1] HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL,BOSTON,MA 02115

[2] BERLEX LABS INC,MORRISTOWN,NJ 07927

[3] GENENTECH INC,DEPT PROT ENGN,S SAN FRANCISCO,CA 94080

来源：

BIOCHEMISTRY | 1993年 / 32卷 / 01期

关键词：

D O I：

10.1021/bi00052a036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The pairing of the cysteines indisulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet aggregation. Kistrin belongs to a family of homologous proteins found in snake venoms termed disintegrins, all of which have a cysteine content. The disulfide pairing of the 2 cysteines was investigated by chemical analysis, NMR spectroscopy, and distance geometry calculations. The data show that the disulfide pairs are 4-19, 6-14, 13-36, 27-33, 32-57, and 45-64. The various means for assigning the disulfide bonds are described, and the results are compared with the cysteine pairings reported for other disintegrin proteins.

引用

页码：282 / 289

页数：8

共 26 条

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