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Conserved sequence motifs and the structure of the mTOR kinase domain

Sauer, E. and Imseng, S. and Maier, T. and Hall, M. N.. (2013) Conserved sequence motifs and the structure of the mTOR kinase domain. Biochemical Society Transactions, 41 (4). pp. 889-895.

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Official URL: http://edoc.unibas.ch/dok/A6165094

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Abstract

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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Hall)
UniBasel Contributors:Hall, Michael N.
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Portland Press
ISSN:0300-5127
e-ISSN:1470-8752
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:09 Nov 2017 09:38
Deposited On:13 Sep 2013 07:52

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