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Architecture of the human mTORC2 core complex.

Architecture of the human mTORC2 core complex.
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Stuttfeld E, Aylett CHS, Imseng S, Boehringer D, Scaiola A, Sauer E, Hall MN, Maier T, Ban N,


Stuttfeld E, Aylett CHS, Imseng S, Boehringer D, Scaiola A, Sauer E, Hall MN, Maier T, Ban N, (click to view)

Stuttfeld E, Aylett CHS, Imseng S, Boehringer D, Scaiola A, Sauer E, Hall MN, Maier T, Ban N,

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eLife 2018 02 097() doi 10.7554/eLife.33101
Abstract

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.

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