Crystallization and preliminary crystallographic study of Porcine epidemic diarrhea virus main protease in complex with an inhibitor
Identifieur interne : 001765 ( Main/Exploration ); précédent : 001764; suivant : 001766Crystallization and preliminary crystallographic study of Porcine epidemic diarrhea virus main protease in complex with an inhibitor
Auteurs : Yusheng Tan ; Fenghua Wang ; Xia Chen ; Jinshan Wang ; Qi Zhao ; Shuang Li ; Zefang Wang ; Sheng Fu ; Cheng Chen ; Haitao YangSource :
- Acta Crystallographica Section F [ 2053-230X ] ; 2014-12-01.
Abstract
Porcine epidemic diarrhea virus (PEDV) mainly infects neonatal pigs, resulting in significant morbidity and mortality. Owing to problems such as long periods of virus shedding, existing vaccines cannot provide complete protection from PEDV infection. The PEDV genome encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome‐encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of Porcine epidemic diarrhea virus in complex with a Michael acceptor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space group R3, with unit‐cell parameters a = 175.3, b = 175.3, c = 58.7 Å. Two molecules were identified per asymmetric unit.
Url:
DOI: 10.1107/S2053230X14021876
Affiliations:
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Owing to problems such as long periods of virus shedding, existing vaccines cannot provide complete protection from PEDV infection. The PEDV genome encodes two polyprotein precursors required for genome replication and transcription. Each polyprotein undergoes extensive proteolytic processing, resulting in functional subunits. This process is mainly mediated by its genome‐encoded main protease, which is an attractive target for antiviral drug design. In this study, the main protease of Porcine epidemic diarrhea virus in complex with a Michael acceptor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space group R3, with unit‐cell parameters a = 175.3, b = 175.3, c = 58.7 Å. Two molecules were identified per asymmetric unit.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Chen, Cheng" sort="Chen, Cheng" uniqKey="Chen C" first="Cheng" last="Chen">Cheng Chen</name><name sortKey="Chen, Xia" sort="Chen, Xia" uniqKey="Chen X" first="Xia" last="Chen">Xia Chen</name><name sortKey="Fu, Sheng" sort="Fu, Sheng" uniqKey="Fu S" first="Sheng" last="Fu">Sheng Fu</name><name sortKey="Li, Shuang" sort="Li, Shuang" uniqKey="Li S" first="Shuang" last="Li">Shuang Li</name><name sortKey="Tan, Yusheng" sort="Tan, Yusheng" uniqKey="Tan Y" first="Yusheng" last="Tan">Yusheng Tan</name><name sortKey="Wang, Fenghua" sort="Wang, Fenghua" uniqKey="Wang F" first="Fenghua" last="Wang">Fenghua Wang</name><name sortKey="Wang, Jinshan" sort="Wang, Jinshan" uniqKey="Wang J" first="Jinshan" last="Wang">Jinshan Wang</name><name sortKey="Wang, Zefang" sort="Wang, Zefang" uniqKey="Wang Z" first="Zefang" last="Wang">Zefang Wang</name><name sortKey="Yang, Haitao" sort="Yang, Haitao" uniqKey="Yang H" first="Haitao" last="Yang">Haitao Yang</name><name sortKey="Zhao, Qi" sort="Zhao, Qi" uniqKey="Zhao Q" first="Qi" last="Zhao">Qi Zhao</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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