期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 29, 期 -, 页码 134-142出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.11.003
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资金
- LMB Cambridge International Studentship
- Cambridge Overseas Trust
- Trinity College Cambridge
- UK MRC [MC_U105184308]
- MRC [MC_U105184308] Funding Source: UKRI
- Medical Research Council [MC_U105184308] Funding Source: researchfish
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.
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