Molecular chaperones: How J domains turn on Hsp70s

被引：99

作者：

Kelley, WL ^{[1
]}

机构：

[1] Univ Geneva, CMU, Dept Biochim Med, CH-1211 Geneva 4, Switzerland

来源：

CURRENT BIOLOGY | 1999年 / 9卷 / 08期

关键词：

D O I：

10.1016/S0960-9822(99)80185-7

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：

Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.

引用

页码：R305 / R308

页数：4

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