A chaperone with a hydrophilic surface

被引：13

作者：

Cowan, NJ ^{[1
]}

Lewis, SA ^{[1
]}

机构：

[1] NYU, Med Ctr, Dept Biochem, New York, NY 10016 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1999年 / 6卷 / 11期

关键词：

D O I：

10.1038/14870

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 folding of native tubulin involves at least seven different chaperone proteins: prefoldin, the cytosolic chaperonin CCT and five tubulin-specific chaperone proteins named cofactors A-E, The structure of the yeast homolog of cofactor A, Rbl2p, shows it to be a dimer with largely hydrophilic surfaces, reflecting the fact that it interacts with quasi-native, not unfolded, beta-tubulin.

引用

页码：990 / 991

页数：2

共 9 条

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