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Publication Date:
February 2012
ISSN:
1868-503X
DOI:
10.1515/bmc.2011.052

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Editor-in-Chief: Jollès, Pierre / Jörnvall, Hans / Mansuy, Isabelle

null Avila, Jesus / Bollen, Mathieu / Bonetto, Valentina / Cera, Enrico / Jorgensen, Erik / Lagasse, Eric / Norman, Robert / Pinna, Lorenzo / Raghavan, K. Vijay / Venetianer, Pal / Wahli, Walter

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From head to toe of the norovirus 3C-like protease

1Department of Virology II, National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashi-Murayama, Tokyo 208-0011, Japan

Citation Information: BioMolecular Concepts. Volume 3, Issue 1, Pages 41–56, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: 10.1515/bmc.2011.052, February 2012

Publication History:

Received: 16/06/2011;
Accepted: 02/11/2011;
Published Online: 26/02/2012

Abstract

Noroviruses are major causative agents of viral gastroenteritis in humans. Currently, there are no therapeutic medications to treat noroviral infections, nor are there effective vaccines against these pathogens. The viral 3C-like protease is solely responsible for the maturation of viral protein components. The crystal structures of the proteases were resolved at high atomic resolution. The protease was also explored by means of mutagenesis. These studies revealed the active-site amino acid residues and factors determining and affecting substrate specificity as well as the principle of architecting the protease molecule. The possible mechanism of proteolysis was also suggested. Consideration of the data accumulated thus far will be useful for development of therapeutic drugs targeting the viral protease.

Keywords: crystal structure; mutagenesis; norovirus; protease; proteolysis

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