Architecture of human mTOR complex 1
What this study shows
Cryo-EM architecture of human mTORC1 reveals its dimeric organization and active site access.
At a glance
| Evidence type | M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Cryo-EM structure) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is. |
| Study type | 5 - Mechanistic / In Vitro |
| Model system | Cryo-EM structure |
| Journal | Science |
| Year | 2015 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1126/science.aaa3870 · PMID 26678875 |
Extracted findings
These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.
| Intervention | Structural (cryo-EM) |
| Target | mTORC1 (mTOR/Raptor/mLST8/FKBP-rapamycin) |
| Model | Cryo-EM structure |
| Effect | Resolves the architecture of human mTORC1 bound to FKBP-rapamycin |
In the Atlas
Related topics
Links in the pathway map
- Supports FKBP12 binds mTORC1
More studies on this topic
- Structure of the human mTOR complex I and its implications for rapamycin inhibition (2010)
- Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP (1996)
- mTOR kinase structure, mechanism and regulation (2013)
- Tor forms a dimer through an N-terminal helical solenoid with a complex topology (2016)
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