Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2

The target of rapamycin (TOR) kinase assembles into two distinct multiprotein complexes, conserved across eukaryote evolution. In contrast to TOR complex 1 (TORC1), TORC2 kinase activity is not inhibited by the macrolide rapamycin. Here, we present the structure of Saccharomyces cerevisiae TORC2 determined by electron cryo-microscopy. TORC2 contains six subunits assembling into a 1.4 MDa rhombohedron. Tor2 and Lst8 form the common core of both TOR complexes.

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Karuppasamy, M., et al. (2017). Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2. Nature communications. https://doi.org/10.1038/s41467-017-01862-0

@article{KAR2017,
  author       = {Karuppasamy, M. and Schaffitzel, C. and others},
  title        = {{Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2}},
  journal      = {Nature communications},
  year         = {2017},
  doi          = {10.1038/s41467-017-01862-0},
  note         = {PMID: 29170376},
}

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 KAR2017) [Data set]. https://mtor-atlas.org/study/KAR2017/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_KAR2017,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record KAR2017},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/KAR2017/},
  doi          = {10.5281/zenodo.22059963}
}