Imperial College London
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DrChristopherAylett

Faculty of Medicine, Department of Infectious Disease

Research Fellow
 
 
 
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Contact

 

+44 (0)20 7594 3862c.aylett

 
 
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Location

 

6.40bFlowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Aylett:2016:10.1126/science.aaa3870,
author = {Aylett, CHS and Sauer, E and Imseng, S and Boehringer, D and Hall, MN and Ban, N and Maier, T},
doi = {10.1126/science.aaa3870},
journal = {Science},
pages = {48--52},
title = {Architecture of human mTOR complex 1.},
url = {http://dx.doi.org/10.1126/science.aaa3870},
volume = {351},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Target of rapamycin (TOR), a conserved protein kinase and central controller of cell growth, functions in two structurally and functionally distinct complexes: TORC1 and TORC2. Dysregulation of mammalian TOR (mTOR) signaling is implicated in pathologies that include diabetes, cancer, and neurodegeneration. We resolved the architecture of human mTORC1 (mTOR with subunits Raptor and mLST8) bound to FK506 binding protein (FKBP)-rapamycin, by combining cryo-electron microscopy at 5.9 angstrom resolution with crystallographic studies of Chaetomium thermophilum Raptor at 4.3 angstrom resolution. The structure explains how FKBP-rapamycin and architectural elements of mTORC1 limit access to the recessed active site. Consistent with a role in substrate recognition and delivery, the conserved amino-terminal domain of Raptor is juxtaposed to the kinase active site.
AU  - Aylett,CHS
AU  - Sauer,E
AU  - Imseng,S
AU  - Boehringer,D
AU  - Hall,MN
AU  - Ban,N
AU  - Maier,T
DO  - 10.1126/science.aaa3870
EP  - 52
PY  - 2016///
SN  - 1095-9203
SP  - 48
TI  - Architecture of human mTOR complex 1.
T2  - Science
UR  - http://dx.doi.org/10.1126/science.aaa3870
UR  - https://www.ncbi.nlm.nih.gov/pubmed/26678875
UR  - https://science.sciencemag.org/content/351/6268/48/
VL  - 351
ER  -
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