Folding and unfolding for binding: large-scale protein dynamics in protein-protein interactions

被引:5
|
作者
Roberts, G. C. K. [1 ]
机构
[1] Univ Leicester, Dept Biochem, Henry Wellcome Labs Struct Biol, Leicester LE1 9HN, Leics, England
基金
英国惠康基金;
关键词
folded protein; guanine nucleotide dissociation inhibitor (GDI); Rho GTPase; protein-protein interaction; talin; vinculin;
D O I
10.1042/BST0340971
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 role of dynamics in the function of proteins, from enzymes to signalling proteins, is widely recognized. in many cases, the dynamic process is a relatively localized one, involving motion of a limited number of key residues, while in others large-scale domain movements may be involved. These motions all take place within the context of a folded protein; however, there is increasing evidence for the existence of some proteins where a transition between folded and unfolded structures is required for function.
引用
收藏
页码:971 / 974
页数:4
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