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双位膜蛋白跨膜α螺旋之间发生的寡聚化的结构方面。

Structural aspects of oligomerization taking place between the transmembrane alpha-helices of bitopic membrane proteins.

作者信息

Arkin Isaiah T

机构信息

Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Givat-Ram, Jerusalem, Israel.

出版信息

Biochim Biophys Acta. 2002 Oct 11;1565(2):347-63. doi: 10.1016/s0005-2736(02)00580-1.

DOI:10.1016/s0005-2736(02)00580-1
PMID:12409206
Abstract

Recent advances in biophysical methods have been able to shed more light on the structures of helical bundles formed by the transmembrane segments of bitopic membrane proteins. In this manuscript, I attempt to review the biological importance and diversity of these interactions, the energetics of bundle formation, motifs capable of inducing oligomerization and methods capable of detecting, solving and predicting the structures of these oligomeric bundles. Finally, the structures of the best characterized instances of transmembrane alpha-helical bundles formed by bitopic membrane proteins are described in detail.

摘要

生物物理方法的最新进展已经能够更深入地揭示由双位膜蛋白的跨膜片段形成的螺旋束结构。在本手稿中,我试图综述这些相互作用的生物学重要性和多样性、束形成的能量学、能够诱导寡聚化的基序以及能够检测、解析和预测这些寡聚束结构的方法。最后,详细描述了由双位膜蛋白形成的跨膜α-螺旋束的最具特征实例的结构。

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