Hussey, R.J., Coates, L., Gill, R.S., Wright, J. Neville, Sarwar, M., Coker, S., Erskine, P.T., Cooper, J.B., Wood, S.P., Clarke, I.N., Lambden, P.R., Broadbridge, R. and Shoolingin-Jordan, P.M.
Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor
Acta Crystallographica Section F: Structural Biology Communications, 66, (11), . (doi:10.1107/S1744309110039059). (PMID:21045318).
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Noroviruses are the predominant cause of human epidemic nonbacterial gastroenteritis. Viral replication requires a cysteine protease that cleaves a 200?kDa viral polyprotein into its constituent functional parts. Here, the crystallization of the recombinant protease from the Southampton norovirus is described. Whilst the native crystals were found to diffract only to medium resolution (2.9?Å), cocrystals of an inhibitor complex diffracted X-rays to 1.7?Å resolution. The polypeptide inhibitor (Ac-EFQLQ-propenyl ethyl ester) possesses an amino-acid sequence designed to match the substrate specificity of the enzyme, but was synthesized with a reactive Michael acceptor group at the C-terminal end.
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