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TitleBinding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.
Journal, issue, pagesJ. Mol. Biol., Vol. 385, Page 1142-1155, Year 2009
Publish dateMar 13, 2008 (structure data deposition date)
AuthorsGallo, M. / Pennestri, M. / Bottomley, M.J. / Barbato, G. / Eliseo, T. / Paci, M. / Narjes, F. / De Francesco, R. / Summa, V. / Koch, U. ...Gallo, M. / Pennestri, M. / Bottomley, M.J. / Barbato, G. / Eliseo, T. / Paci, M. / Narjes, F. / De Francesco, R. / Summa, V. / Koch, U. / Bazzo, R. / Cicero, D.O.
External linksJ. Mol. Biol. / PubMed:19061898
MethodsNMR (solution)
Structure data

PDB-2k1q:
NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitor
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • hepatitis c virus
KeywordsVIRAL PROTEIN / SERINE PROTEASE / NS3 / HEPATITIS C VIRUS / NON COVALENT INHIBITOR / Envelope protein / Helicase / Hydrolase / Nucleotide-binding / RNA replication / Transmembrane

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