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{Imseng:2018:10.1016/j.sbi.2018.03.010,
author = {Imseng, S and Aylett, CHS and Maier, T},
doi = {10.1016/j.sbi.2018.03.010},
journal = {Current Opinion in Structural Biology},
pages = {177--189},
title = {Architecture and activation of phosphatidylinositol 3-kinase related kinases},
url = {http://dx.doi.org/10.1016/j.sbi.2018.03.010},
volume = {49},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The phosphatidylinositol 3-kinase related protein kinases (PIKKs) are key to the regulation of a variety of eukaryotic cellular processes including DNA repair and growth regulation. While these massive proteins had long resisted structural analysis, recent advances in electron cryo-microscopy have now facilitated structural analysis of the major examples of PIKKs, including mTOR, DNA-PK, ATM, ATR and TRAPP/Tra1. In these PIKKs, the carboxy-terminal kinase domains and their proximal regions are structurally conserved. The structural organization of their extensive amino-terminal repeat regions, however, as well as their oligomeric organization and their interactions with accessory proteins, differ markedly amongst PIKKs. This architectural divergence provides the structural basis for the complex regulatory roles and functional diversity of PIKKs.
AU  - Imseng,S
AU  - Aylett,CHS
AU  - Maier,T
DO  - 10.1016/j.sbi.2018.03.010
EP  - 189
PY  - 2018///
SN  - 0959-440X
SP  - 177
TI  - Architecture and activation of phosphatidylinositol 3-kinase related kinases
T2  - Current Opinion in Structural Biology
UR  - http://dx.doi.org/10.1016/j.sbi.2018.03.010
UR  - http://hdl.handle.net/10044/1/61645
VL  - 49
ER  -
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