Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 11): 1544-8, 2010 Nov 01.
Article
em En
| MEDLINE
| ID: mdl-21045318
ABSTRACT
Noroviruses are the predominant cause of human epidemic nonbacterial gastroenteritis. Viral replication requires a cysteine protease that cleaves a 200â
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 (2.9â
Å), cocrystals of an inhibitor complex diffracted X-rays to 1.7â
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Inibidores de Proteases
/
Norovirus
/
Domínios e Motivos de Interação entre Proteínas
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2010
Tipo de documento:
Article
País de afiliação:
Reino Unido