Molecular chaperones: Structure of a protein disaggregase

被引：88

作者：

Mogk, A ^{[1
]}

Bukau, B ^{[1
]}

机构：

[1] Heidelberg Univ, 1ZMBH, D-69120 Heidelberg, Germany

来源：

CURRENT BIOLOGY | 2004年 / 14卷 / 02期

关键词：

D O I：

10.1016/j.cub.2003.12.051

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.

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收藏

页码：R78 / R80

页数：3

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