@article{Stuttfeld:2018:10.7554/eLife.33101,
author = {Stuttfeld, E and Aylett, CH and Imseng, S and Boehringer, D and Scaiola, A and Sauer, E and Hall, MN and Maier, T and Ban, N},
doi = {10.7554/eLife.33101},
journal = {eLife},
title = {Architecture of the human mTORC2 core complex},
url = {http://dx.doi.org/10.7554/eLife.33101},
volume = {7},
year = {2018}
}

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TY  - JOUR
AB  - 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.
AU  - Stuttfeld,E
AU  - Aylett,CH
AU  - Imseng,S
AU  - Boehringer,D
AU  - Scaiola,A
AU  - Sauer,E
AU  - Hall,MN
AU  - Maier,T
AU  - Ban,N
DO  - 10.7554/eLife.33101
PY  - 2018///
SN  - 2050-084X
TI  - Architecture of the human mTORC2 core complex
T2  - eLife
UR  - http://dx.doi.org/10.7554/eLife.33101
UR  - https://www.ncbi.nlm.nih.gov/pubmed/29424687
UR  - http://hdl.handle.net/10044/1/61156
VL  - 7
ER  - 

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