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在脂质双分子层内切割蛋白质:类菱形蛋白酶的结构与作用机制

Cutting proteins within lipid bilayers: rhomboid structure and mechanism.

作者信息

Lemberg Marius K, Freeman Matthew

机构信息

MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.

出版信息

Mol Cell. 2007 Dec 28;28(6):930-40. doi: 10.1016/j.molcel.2007.12.003.

DOI:10.1016/j.molcel.2007.12.003
PMID:18158892
Abstract

Rhomboids were only discovered to be novel proteases in 2001, but progress on understanding this newest family of intramembrane proteases has been rapid. They are now the best characterized of these rather mysterious enzymes that cleave transmembrane domains within the lipid bilayer. In particular, the biochemical analysis of solubilized rhomboids and, most recently, a flurry of high-resolution crystal structures, have led to real insight into their enzymology. Long-standing questions about how it is possible for a water-requiring proteolytic reaction to occur in the lipid bilayer are now answered for the rhomboids. Intramembrane proteases, which control many medically important biological processes, have made the transition from rather heretical outsiders to novel enzymes that are becoming well understood.

摘要

菱形蛋白酶直到2001年才被发现是新型蛋白酶,但在理解这个最新的膜内蛋白酶家族方面进展迅速。它们现在是这些相当神秘的酶中特征最明确的,这些酶可在脂质双分子层内切割跨膜结构域。特别是,对可溶菱形蛋白酶的生化分析以及最近一系列高分辨率晶体结构,使人们对其酶学有了真正的深入了解。关于在脂质双分子层中如何发生需要水的蛋白水解反应这个长期存在的问题,现在菱形蛋白酶已经给出了答案。控制许多医学上重要生物学过程的膜内蛋白酶,已经从相当异端的局外人转变为正被充分理解的新型酶。

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