Architecture of human mTOR complex 1

Aylett CH, Maier T et al. · 2015 · Science · Atlas ID AYL2015

What this study shows

Cryo-EM architecture of human mTORC1 reveals its dimeric organization and active site access.

Abstract

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Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution.

Read the full abstract on PubMed →

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	2026-08-22
Source	DOI 10.1126/science.aaa3870 · PMID 26678875

Extracted findings

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

Cite this paper

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Aylett, C. H., et al. (2015). Architecture of human mTOR complex 1. Science. https://doi.org/10.1126/science.aaa3870

@article{AYL2015,
  author       = {Aylett, C. H. and Maier, T. and others},
  title        = {{Architecture of human mTOR complex 1}},
  journal      = {Science},
  year         = {2015},
  doi          = {10.1126/science.aaa3870},
  note         = {PMID: 26678875},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record AYL2015) [Data set]. https://mtor-atlas.org/study/AYL2015/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_AYL2015,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record AYL2015},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/AYL2015/},
  doi          = {10.5281/zenodo.22059963}
}