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PCI蛋白折叠的结构生物学

Structural biology of the PCI-protein fold.

作者信息

Ellisdon Andrew M, Stewart Murray

机构信息

Department of Biochemistry and Molecular Biology; Monash University; Clayton, Victoria, Australia.

MRC Laboratory of Molecular Biology; Cambridge, UK.

出版信息

Bioarchitecture. 2012 Jul-Aug;2(4):118-23. doi: 10.4161/bioa.21131. Epub 2012 Jul 1.

Abstract

The PCI fold is based on a stack of α-helices topped with a winged-helix domain and is found in a range of proteins that form central parts of large complexes such as the proteasome lid, the COP9 signalosome, elongation factor eIF3, and the TREX-2 complex. Recent structural determinations have given intriguing insight into how these folds function both to facilitate the generation of larger proteinaceous assembles and also to interact functionally with nucleic acids.

摘要

PCI折叠结构基于一堆由带翼螺旋结构域封顶的α螺旋,存在于一系列蛋白质中,这些蛋白质构成了大型复合物的核心部分,如蛋白酶体盖子、COP9信号体、延伸因子eIF3和TREX-2复合物。最近的结构测定为这些折叠结构如何发挥作用提供了有趣的见解,既有助于生成更大的蛋白质组装体,又能在功能上与核酸相互作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/97ab/3675071/a73b28dd1e3f/bioa-2-118-g1.jpg

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