热休克蛋白70（Hsp70）伴侣蛋白识别底物的机制。
Mechanism of substrate recognition by Hsp70 chaperones.
作者信息
Erbse A, Mayer M P, Bukau B
机构信息
Zentrum für Molekulare Biologie Heidelberg, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany.
出版信息
Biochem Soc Trans. 2004 Aug;32(Pt 4):617-21. doi: 10.1042/BST0320617.
PMID:15270690
Abstract
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.
摘要
热休克蛋白70（Hsp70）伴侣蛋白在协助蛋白质折叠过程中的作用，依赖于它们以瞬时且受ATP调控的方式与蛋白质底物的短肽段相结合的能力。在本研究中，我们综述了Hsp70蛋白识别底物背后机制的分子细节。
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