| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8320037 | Current Opinion in Structural Biology | 2014 | 9 Pages |
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.
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Authors
Domagoj BaretiÄ, Roger L. Williams,