Structural and mechanistic consequences of polypeptide binding by GroEL

被引:36
作者
Coyle, JE
Jaeger, J
Gross, M
Robinson, CV
Radford, SE [1 ]
机构
[1] Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England
[2] Oxford Ctr Mol Sci, New Chem Lab, Oxford OX1 3QT, England
来源
FOLDING & DESIGN | 1997年 / 2卷 / 06期
基金
英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;
关键词
D O I
10.1016/S1359-0278(97)00046-1
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 remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of proteins constitutes one of the most fascinating molecular recognition events in protein chemistry. Recent structural studies have revealed a possible model for substrate binding by GroEL and a high-resolution image of the GroEL-GroES folding machinery has provided important new insights into our understanding of the mechanism of action of this chaperonin. Studies with a variety of model substrates reveal that the binding of substrate proteins to GroEL is not just a passive event, but can result in significant changes in the structure and stability of the bound polypeptide, the potential impact of this on the mechanism of chaperonin-assisted folding is not fully understood, but provides exciting scope for further experiment.
引用
收藏
页码:R93 / R104
页数:12
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