Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide
| Autor: | J. A. Landro, Charles M. Rice, Paul R. Caron, Stephen P. Chambers, William Markland, Christopher A. Lepre, Morgenstern Kurt A, Chao Lin, Scott L. Harbeson, Murcko Mark A, Ted Fox, Maureen D. Dwyer, John A. Thomson, Joseph L. Kim, Ethan O'malley |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Viral protein Macromolecular Substances Protein Conformation medicine.medical_treatment Hepatitis C virus viruses Population Molecular Sequence Data Beta sheet Hepacivirus Viral Nonstructural Proteins medicine.disease_cause Crystallography X-Ray General Biochemistry Genetics and Molecular Biology Substrate Specificity medicine Amino Acid Sequence education Serine protease education.field_of_study NS3 Protease Binding Sites biology Biochemistry Genetics and Molecular Biology(all) NS2-3 protease Enzyme Activation Zinc Biochemistry biology.protein Sequence Alignment Protein Binding |
| Zdroj: | Cell. 87(2) |
| ISSN: | 0092-8674 |
| Popis: | An estimated 1% of the global human population is infected by hepatitis C viruses (HCVs), and there are no broadly effective treatments for the debilitating progression of chronic hepatitis C. A serine protease located within the HCV NS3 protein processes the viral polyprotein at four specific sites and is considered essential for replication. Thus, it emerges as an attractive target for drug design. We report here the 2.5 A resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic NS4A activator peptide. The protease has a chymotrypsin-like fold and features a tetrahedrally coordinated metal ion distal to the active site. The NS4A peptide intercalates within a β sheet of the enzyme core. |
| Databáze: | OpenAIRE |
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