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Structure paper

TitleDrug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 107, Page 20986-20991, Year 2010
Publish dateMar 12, 2010 (structure data deposition date)
AuthorsRomano, K.P. / Ali, A. / Royer, W.E. / Schiffer, C.A.
External linksProc. Natl. Acad. Sci. USA / PubMed:21084633
MethodsX-ray diffraction
Resolution1.25 - 1.9 Å
Structure data

PDB-3m5l:
Crystal structure of HCV NS3/4A protease in complex with ITMN-191
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-3m5m:
Avoiding drug resistance against HCV NS3/4A protease inhibitors
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3m5n:
Crystal structure of HCV NS3/4A protease in complex with N-terminal product 4B5A
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3m5o:
Crystal structure of HCV NS3/4A protease in complex with N-terminal product 5A5B
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-TSV:
(2R,6S,12Z,13aS,14aR,16aS)-6-[(tert-butoxycarbonyl)amino]-14a-[(cyclopropylsulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8 / inhibitor*YM

ChemComp-SO4:
SULFATE ION

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • hepatitis c virus subtype 1a
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HCV / Hepatitis C Virus / NS3 / protease / drug resistance / serine protease / chimera protein / fusion protein / HYDROLASE-HYDROLASE INHIBITOR complex

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