Gymnastics of Molecular Chaperones

被引：279

作者：

Mayer, Matthias P. ^{[1
]}

机构：

[1] Univ Heidelberg ZMBH, Zentrum Mol Biol, DKFZ ZMBH Allianz, D-69120 Heidelberg, Germany

来源：

MOLECULAR CELL | 2010年 / 39卷 / 03期

关键词：

HSP70 NUCLEOTIDE EXCHANGE; ESCHERICHIA-COLI HSP90; CRYSTAL-STRUCTURE; ATP HYDROLYSIS; IN-VIVO; STRUCTURAL BASIS; CONFORMATIONAL DYNAMICS; EUKARYOTIC CHAPERONIN; ALLOSTERIC REGULATION; SUBSTRATE-BINDING;

D O I：

10.1016/j.molcel.2010.07.012

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 assist folding processes and conformational changes in many proteins. In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families. © 2010 Elsevier Inc.

引用

页码：321 / 331

页数：11

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