Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins

被引：97

作者：

Saibil, H ^{[1
]}

机构：

[1] Univ London Birkbeck Coll, Dept Crystallog, London WC1E 7HX, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2000年 / 10卷 / 02期

关键词：

D O I：

10.1016/S0959-440X(00)00074-9

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：

Newly solved chaperone structures include the thermosome, a group II chaperonin, and a small heat-shock protein. Novel ideas on chaperone mechanism are presented in the forced unfolding hypothesis of GroEL action. Structures of chaperone-pilin complexes reveal the mechanism of chaperone interaction in bacterial pilus assembly and there have been major advances in understanding the structure and function of Hsp 100 unfoldases.

引用

页码：251 / 258

页数：8

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