3D DOMAIN SWAPPING - A MECHANISM FOR OLIGOMER ASSEMBLY

被引：670

作者：

BENNETT, MJ

SCHLUNEGGER, MP

EISENBERG, D

机构：

[1] UNIV CALIF LOS ANGELES,INST MOLEC BIOL,DEPT CHEM & BIOCHEM,LOS ANGELES,CA 90095

[2] UNIV CALIF LOS ANGELES,UCLA DOE,STRUCT BIOL & MOLEC MED LAB,LOS ANGELES,CA 90095

[3] UNIV PENN,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104

来源：

PROTEIN SCIENCE | 1995年 / 4卷 / 12期

关键词：

AGGREGATION; COMPLEMENTATION; OLIGOMER EVOLUTION; PROTEIN DIMERIZATION;

D O I：

10.1002/pro.5560041202

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：

3D domain swapping is a mechanism for forming oligomeric proteins from their monomers. In 3D domain swapping, one domain of a monomeric protein is replaced by the same domain from an identical protein chain. The result is an intertwined dimer or higher oligomer, with one domain of each subunit replaced by the identical domain from another subunit. The swapped ''domain'' can be as large as an entire tertiary globular domain, or as small as an a-helix or a strand of a P-sheet. Examples of 3D domain swapping are reviewed that suggest domain swapping can serve as a mechanism for functional interconversion between monomers and oligomers, and that domain swapping may serve as a mechanism for evolution of some oligomeric proteins. Domain-swapped proteins present examples of a single protein chain folding into two distinct structures.

引用

页码：2455 / 2468

页数：14

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