The atypical serine/threonine kinase mTOR (mammalian target of rapamycin) is a central regulator of cell growth and metabolism. mTOR is part of two multisubunit signalling complexes, mTORC1 and mTORC2. Although many aspects of mTOR signalling are understood, the lack of high-resolution structures impairs a detailed understanding of complex assembly, function and regulation. The structure of the kinase domain is of special interest for the development of mTOR inhibitors as anti-cancer agents. A homology model of the mTOR kinase domain was derived from the structure of PI3Ks (phosphoinositide 3-kinases). More recently, the crystal structure of the catalytic domain of human mTOR was determined, providing long-awaited structural insight into the architecture of mTOR. Interestingly, the homology model predicted several aspects of the crystal structure. In the present paper, we revisit the homology model in the context of the now available crystal structure of the mTOR kinase domain.
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August 2013
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Conference Article|
July 18 2013
Conserved sequence motifs and the structure of the mTOR kinase domain
Evelyn Sauer;
Evelyn Sauer
1Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland
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Stefan Imseng;
Stefan Imseng
1Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland
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Timm Maier;
Timm Maier
1Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland
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Michael N. Hall
Michael N. Hall
1
1Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland
1To whom correspondence should be addressed (emailM.Hall@unibas.ch).
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Publisher: Portland Press Ltd
Received:
June 14 2013
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem Soc Trans (2013) 41 (4): 889–895.
Article history
Received:
June 14 2013
Citation
Evelyn Sauer, Stefan Imseng, Timm Maier, Michael N. Hall; Conserved sequence motifs and the structure of the mTOR kinase domain. Biochem Soc Trans 1 August 2013; 41 (4): 889–895. doi: https://doi.org/10.1042/BST20130113
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