Mechanism of substrate recognition by Hsp70 chaperones

被引：62

作者：

Erbse, A ^{[1
]}

Mayer, MP ^{[1
]}

Bukau, B ^{[1
]}

机构：

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

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2004年 / 32卷

关键词：

ATP hydrolysis; binding; chaperone; DnaJ protein; Hsp70; substrate recognition;

D O I：

10.1042/BST0320617

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 role of Hsp70 (heat-shock protein 70) chaperones in assisting protein-folding processes relies on their ability to associate with short peptide stretches of protein substrates in a transient and ATP-controlled manner. In the present study, we review the molecular details of the mechanism behind substrate recognition by Hsp70 proteins.

引用

页码：617 / 621

页数：5

共 37 条

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