Ellisdon Andrew M, Stewart Murray
Department of Biochemistry and Molecular Biology; Monash University; Clayton, Victoria, Australia.
MRC Laboratory of Molecular Biology; Cambridge, UK.
Bioarchitecture. 2012 Jul-Aug;2(4):118-23. doi: 10.4161/bioa.21131. Epub 2012 Jul 1.
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.
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。
