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Preliminary crystallographic analysis of neuraminidase N2 from a new influenza A virus

tetano

Editor, Senior Moderator
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug 1;69(Pt 8):861-863. Epub 2013 Jul 27.
Preliminary crystallographic analysis of neuraminidase N2 from a new influenza A virus.
Gao F, Bao J.
Source

School of Life Sciences, Sichuan University, Chengdu 610064, People's Republic of China.
Abstract

Influenza virus is a major viral respiratory pathogen that causes yearly epidemics in temperate climates. The H3N2 subtype is one of the major causative agents of severe epidemics and plays a critical role in vaccine development. The neuraminidase (NA) inhibitors oseltamivir and zanamivir are two commercially available NA-targeted competitive antiviral drugs. However, their effectiveness has been compromised by the rapid emergence of resistance. Q136K is a novel mutation in NA which confers resistance to zanamivir. In this study, a Q136K mutant N2 protein was expressed in a baculovirus system and crystals were obtained. The crystal of N2 belonged to space group P212121, with unit-cell parameters a = 109.5, b = 112.8, c = 165.2 ?. Data were collected to 2.4 ? resolution. Four monomers were found in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 3.0 ?3 Da-1 and 59.0%, respectively.
KEYWORDS:

drug resistance, influenza A virus, neuraminidases

PMID:
23908028
[PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/23908028
 
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