The chaperonin folding machine

被引:101
作者
Saibil, HR
Ranson, NA
机构
[1] Univ London Birkbeck Coll, Sch Crystallog, London WC1E 7HX, England
[2] Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England
基金
英国惠康基金;
关键词
D O I
10.1016/S0968-0004(02)02211-9
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
Chaperonins are versatile molecular machines that assist the folding of a wide range of substrate proteins. They harness an ATPase cycle to control access of non-native proteins to hydrophobic binding sites. ATP binding promotes large conformational changes that partially bury the hydrophobic sites and initiate the binding of a co-chaperonin, creating closed and open cavities. Non-native proteins progress towards the native fold during their confinement in these cavities, and are then released by the allosteric action of ATP.
引用
收藏
页码:627 / 632
页数:6
相关论文
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