Architecture of the human mTORC2 core complex (mTOR-Rictor-SIN1-mLST8).
| Evidence tier | D Mechanistic / in vitro / review |
| Study type | 5 - Mechanistic / In Vitro |
| Model system | Cryo-EM structure |
| Journal | eLife |
| Year | 2018 |
| Peer reviewed | Yes |
| Source | DOI 10.7554/eLife.33101 · PMID 29424687 · Free full text (PMC5837792) |
The mammalian target of rapamycin (mTOR) is a key protein kinase controlling cellular metabolism and growth. It is part of the two structurally and functionally distinct multiprotein complexes mTORC1 and mTORC2. Dysregulation of mTOR occurs in diabetes, cancer and neurological disease. We report the architecture of human mTORC2 at intermediate resolution, revealing a conserved binding site for accessory proteins on mTOR and explaining the structural basis for the rapamycin insensitivity of the complex.
| Intervention | Structural (cryo-EM) |
| Target | mTORC2 core |
| Model | Cryo-EM structure |
| Effect | Architecture of the human mTORC2 core complex, revealing a conserved accessory-protein binding site |