Imperial College London

ProfessorStephenCurry

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 7632s.curry Website

 
 
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Assistant

 

Mrs Faaria Henry +44 (0)20 7594 1919

 
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Location

 

404ASir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@techreport{Yang:2016:10.7287/peerj.preprints.1750v1,
author = {Yang, J and Leen, EN and Maree, FF and Curry, S},
doi = {10.7287/peerj.preprints.1750v1},
publisher = {PeerJ Preprints},
title = {Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus},
url = {http://dx.doi.org/10.7287/peerj.preprints.1750v1},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - RPRT
AB - The replication of foot-and-mouth disease virus (FMDV) is dependent on the virus-encoded 3C protease (3Cpro). As in other picornaviruses, 3Cpro performs most of the proteolytic processing of the polyprotein expressed from the single open reading frame in the RNA genome of the virus. Previous work revealed that the 3Cpro from serotype A – one of the seven serotypes of FMDV – adopts a trypsin-like fold. Phylogenetically the FMDV serotypes are grouped into two clusters, with O, A, C, and Asia 1 in one, and the three South African Territories serotypes, (SAT-1, SAT-2 and SAT-3) in another. We report here the cloning, expression and purification of 3C proteases from four SAT serotype viruses (SAT2/GHA/8/91, SAT1/NIG/5/81, SAT1/UGA/1/97, and SAT2/ZIM/7/83) and the crystal structure at 3.2 Å resolution of 3Cpro from SAT2/GHA/8/91).
AU - Yang,J
AU - Leen,EN
AU - Maree,FF
AU - Curry,S
DO - 10.7287/peerj.preprints.1750v1
PB - PeerJ Preprints
PY - 2016///
TI - Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus
UR - http://dx.doi.org/10.7287/peerj.preprints.1750v1
UR - http://www.imperial.ac.uk/people/s.curry
UR - https://peerj.com/preprints/1750/
UR - http://hdl.handle.net/10044/1/29642
ER -