PIKKs - the solenoid nest where partners and kinases meet
PIKKs - the solenoid nest where partners and kinases meet
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DOI：
10.1016/j.sbi.2014.11.003
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发表时间：
2014-12-01
影响因子：
6.8
通讯作者：
Williams, Roger L.
中科院分区：
文献类型：
--
作者：
Baretic, Domagoj;Williams, Roger L.
与mLST 8复合的截短mTOR的最新结构为理解所有磷酸肌醇3-激酶（PI 3 K）相关激酶（PIKK）：mTOR、ATM、ATR、SMG-1、TRRAP和DNA-PK提供了基本框架。PIKK激酶结构域被FAT结构域包围，FAT结构域是存在于所有PIKK中的螺旋螺线管。PIKK在FAT结构域的N-末端还具有广泛的螺旋螺线管，其结构信息有限。该N-末端螺旋螺线管对于与PIKK相关的结合蛋白调节其活性和细胞定位是必需的。
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.