Imperial College London
Alternate

ProfessorMichaelSternberg

Faculty of Natural Sciences, Department of Life Sciences

Director, Systems Biology and Bioinformatics Centre
 
 
 
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Contact

 

+44 (0)20 7594 5212m.sternberg Website

 
 
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Location

 

306Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Greener:2017:10.1016/j.sbi.2017.10.002,
author = {Greener, J and sternberg, MJE},
doi = {10.1016/j.sbi.2017.10.002},
journal = {Current Opinion in Structural Biology},
pages = {1--8},
title = {Structure-based prediction of protein allostery},
url = {http://dx.doi.org/10.1016/j.sbi.2017.10.002},
volume = {50},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Allostery is the functional change at one site on a protein caused by a change at a distant site. In order for the benefits of allostery to be taken advantage of, both for basic understanding of proteins and to develop new classes of drugs, the structure-based prediction of allosteric binding sites, modulators and communication pathways is necessary. Here we review the recently emerging field of allosteric prediction, focusing mainly on computational methods. We also describe the search for cryptic binding pockets and attempts to design allostery into proteins. The development and adoption of such methods is essential or the long-preached potential of allostery will remain elusive.
AU  - Greener,J
AU  - sternberg,MJE
DO  - 10.1016/j.sbi.2017.10.002
EP  - 8
PY  - 2017///
SN  - 0959-440X
SP  - 1
TI  - Structure-based prediction of protein allostery
T2  - Current Opinion in Structural Biology
UR  - http://dx.doi.org/10.1016/j.sbi.2017.10.002
UR  - http://hdl.handle.net/10044/1/51537
VL  - 50
ER  -
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