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Kuhn Lab at The Scripps Research Institute. > KSPublications > Crystal structure of a monomeric form of SARS-CoV endonuclease nsp15 suggests a role for hexamerization as an allosteric switch  

KSPublications: Crystal structure of a monomeric form of SARS-CoV endonuclease nsp15 suggests a role for hexamerization as an allosteric switch

Title

Crystal structure of a monomeric form of SARS-CoV endonuclease nsp15 suggests a role for hexamerization as an allosteric switch 

Authors

Joseph JS, et al. 

Abstract

Journal

Journal of Virology 

Date

2/27/2007 

Link

Link 

Reference

Joseph JS, Saikatendu KS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P. “Crystal structure of a monomeric form of SARS-CoV endonuclease nsp15 suggests a role for hexamerization as an allosteric switchJ. Virol. In press (2007).

PMID

17409150 

Keyword

FSPS 

TSRI Number

18649 
Attachments
Created at 2/27/2007 2:14 PM  by Sophie Coon 
Last modified at 10/1/2008 9:53 AM  by System Account