Crystallization and preliminary crystallographic study ofPorcine epidemic diarrhea virusmain protease in complex with an inhibitor
| Autor: | Qi Zhao, Yusheng Tan, Cheng Chen, Jinshan Wang, Li Shuang, Xia Chen, Haitao Yang, Fu Sheng, Zefang Wang, Fenghua Wang |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
medicine.drug_class
medicine.medical_treatment Biophysics Biology Crystallography X-Ray Virus Replication Biochemistry Genome Microbiology Structural Biology Transcription (biology) Genetics medicine Protease Inhibitors Viral shedding Protease Porcine epidemic diarrhea virus Condensed Matter Physics biology.organism_classification Virology NS2-3 protease Viral replication Crystallization Communications Antiviral drug Crystallization Peptide Hydrolases |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x14021876 |
| Popis: | 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 ofPorcine epidemic diarrhea virusin complex with a Michael acceptor was crystallized. The complex crystals diffracted to 2.5 Å resolution and belonged to space groupR3, with unit-cell parametersa= 175.3,b= 175.3,c= 58.7 Å. Two molecules were identified per asymmetric unit. |
| Databáze: | OpenAIRE |
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