Tor forms a dimer through an N-terminal helical solenoid with a complex topology
What this study shows
Cryo-EM shows TOR dimerizes through an N-terminal helical solenoid, informing mTORC1 architecture.
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 | Nature communications |
| Year | 2016 |
| Peer reviewed | Yes |
| Record last updated | 2026-10-01 |
| Source | DOI 10.1038/ncomms11016 · PMID 27072897 · Free full text (PMC4833857) |
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 | TOR / Lst8 |
| Model | Cryo-EM structure |
| Effect | Tor-Lst8 heterodimers assemble into a dyad-symmetric dimer via Tor-Tor interactions (N-terminal solenoid) |
In the Atlas
Related topics
More studies on this topic
- Architecture of human mTOR complex 1 (2015)
- Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1 (2006)
- GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR (2003)
- Structure of the human mTOR complex I and its implications for rapamycin inhibition (2010)
Was this page useful?
Thank you. Your answer was counted anonymously.