How far divergent evolution goes in proteins

被引:208
作者
Murzin, AG [1 ]
机构
[1] MRC Ctr, Ctr Prot Engn, Cambridge CB2 2QH, England
关键词
D O I
10.1016/S0959-440X(98)80073-0
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
In theory, mutations of protein sequences may eventually generate different functions as well as different structures. The observation of such records of protein evolution have been obscured by the dissipation of memory about the ancestors. In the past year, new advances in our understanding of divergent evolution were allowed by new protein structure determinations, including the ClpP protease, steroid Delta-isomerase, carboxypeptidase G(2), the thrombin inhibitor triabin and the chloroplast Rieske protein. There is strong evidence for their distant homology with proteins of known structure despite significant functional or structural differences.
引用
收藏
页码:380 / 387
页数:8
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