Structure of rhodocetin reveals noncovalently bound heterodimer interface

被引：19

作者：

Paaventhan, P

Kong, CG

Joseph, JS

Chung, MCM

Kolatkar, PR ^{[1
]}

机构：

[1] Genome Inst Singapore, Singapore 138672, Singapore

[2] Inst Mol & Cell Biol, Singapore 117609, Singapore

[3] Scripps Res Inst, La Jolla, CA 92037 USA

[4] Natl Univ Singapore, Fac Med, Dept Biochem, Singapore 117597, Singapore

来源：

PROTEIN SCIENCE | 2005年 / 14卷 / 01期

关键词：

platelet aggregation inhibitor; Calloselasma rhodostoma; heterodimer; C-type lectin-like protein; domain swapping;

D O I：

10.1110/ps.04945605

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：

Rhodocetin is a unique heterodimer consisting of alpha- and beta-subunits of 133 and 129 residues, respectively. The molecule, purified front the crude venom of the Malayan pit viper, Calloselasma rhodostoma, functions as an inhibitor of collagen-induced aggregation. Rhodocetin has been shown to have activity only when present as a dimer. The dimer is formed without an intersubunit disulfide bridge. unlike all the other Ca2+-dependent lectin-like proteins. We report here the 1.9 A resolution Structure of rhodocetin, which reveals the compensatory interactions that occur in the absence of the disulfide bridge to preserve activity.

引用

页码：169 / 175

页数：7

共 24 条

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