Three-dimensional domain swapping in homooligomeric proteins and its functional significance

被引：15
|
作者：
Nagradova, NK [1 ]
机构：
[1] Moscow MV Lomonosov State Univ, Belozersky Inst Phys Chem Biol, Moscow 119992, Russia
来源：
BIOCHEMISTRY-MOSCOW | 2002年 / 67卷 / 08期
基金：
俄罗斯基础研究基金会;
关键词：
three-dimensional domain swapping; oligomeric structure; domains; protein-protein interactions; aggregation;
D O I：
10.1023/A:1019958402194
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 the process of oligomeric structure formation through a mechanism of three-dimensional domain swapping, one domain of a monomeric protein is replaced by the same domain from an identical monomer. The swapped "domain" can represent an entire tertiary globular domain or an element of secondary protein structure, such as an (x-helix or a P-strand. Different examples of three-dimensional domain swapping are reviewed; the functional importance of this phenomenon and its role in the development of new properties by some proteins in the process of evolution are considered. The contribution of three-dimensional domain swapping to the formation of linear protein polymers and amyloids is discussed.
引用
收藏
页码：839 / 849
页数：11
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