PIKKs——伙伴和激酶相遇的螺旋巢。

PIKKs--the solenoid nest where partners and kinases meet.

机构信息

Laboratory of Molecular Biology, Medical Research Council, Francis Crick Avenue, Cambridge CB2 0QH, UK.

出版信息

Curr Opin Struct Biol. 2014 Dec;29:134-42. doi: 10.1016/j.sbi.2014.11.003. Epub 2014 Dec 3.

DOI:10.1016/j.sbi.2014.11.003

Abstract

The recent structure of a truncated mTOR in a complex with mLST8 has provided a basic framework for understanding all of the phosphoinositide 3-kinase (PI3K)-related kinases (PIKKs): mTOR, ATM, ATR, SMG-1, TRRAP and DNA-PK. The PIKK kinase domain is encircled by the FAT domain, a helical solenoid that is present in all PIKKs. PIKKs also have an extensive helical solenoid N-terminal to the FAT domain for which there is limited structural information. This N-terminal helical solenoid is essential for binding proteins that associate with the PIKKs to regulate their activity and cellular localization.

摘要

最近，mTOR 与 mLST8 复合物的截断结构为理解所有磷脂酰肌醇 3-激酶（PI3K）相关激酶（PIKKs）提供了一个基本框架：mTOR、ATM、ATR、SMG-1、TRRAP 和 DNA-PK。PIKK 的激酶结构域被 FAT 结构域包围，FAT 结构域是所有 PIKK 中都存在的螺旋螺线管。PIKK 还具有 FAT 结构域之前的广泛螺旋螺线管 N 端，但其结构信息有限。该 N 端螺旋螺线管对于结合与 PIKK 相关的蛋白以调节其活性和细胞定位是必需的。