STRUCTURAL MECHANISMS FOR DOMAIN MOVEMENTS IN PROTEINS

被引：677

作者：

GERSTEIN, M

LESK, AM

CHOTHIA, C

机构：

[1] UNIV CAMBRIDGE,DEPT HAEMATOL,MRC,MOLEC BIOL LAB,CAMBRIDGE CB2 2QH,ENGLAND

[2] CAMBRIDGE CTR PROT ENGN,CAMBRIDGE CB2 2QH,CAMBS,ENGLAND

来源：

BIOCHEMISTRY | 1994年 / 33卷 / 22期

关键词：

D O I：

10.1021/bi00188a001

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：

We survey all the known instances of domain movements in proteins for which there is crystallographic evidence for the movement. We explain these domain movements in terms of the repertoire of low-energy conformation changes that are known to occur in proteins. We first describe the basic elements of this repertoire, hinge and shear motions, and then show how the elements of the repertoire can be combined to produce domain movements. We emphasize that the elements used in particular proteins are determined mainly by the structure of the interfaces between the domains.

引用

收藏

页码：6739 / 6749

页数：11

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