3D结构域交换：一种寡聚体组装机制。
3D domain swapping: a mechanism for oligomer assembly.
作者信息
Bennett M J, Schlunegger M P, Eisenberg D
机构信息
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104-6059, USA.
出版信息
Protein Sci. 1995 Dec;4(12):2455-68. doi: 10.1002/pro.5560041202.
Abstract
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 alpha-helix or a strand of a beta-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.
摘要
3D结构域交换是一种由单体形成寡聚蛋白的机制。在3D结构域交换中，单体蛋白的一个结构域被来自相同蛋白链的相同结构域所取代。结果是形成一个相互缠绕的二聚体或更高阶的寡聚体，每个亚基的一个结构域被来自另一个亚基的相同结构域所取代。交换的“结构域”可以大到整个三级球状结构域，也可以小到一个α螺旋或一条β折叠链。本文综述了3D结构域交换的实例，这些实例表明结构域交换可作为单体和寡聚体之间功能相互转换的一种机制，并且结构域交换可能是某些寡聚蛋白进化的一种机制。结构域交换蛋白展示了单条蛋白链折叠成两种不同结构的实例。
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