2hal
From Proteopedia
An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors
Template:ABSTRACT PUBMED 16860823
About this Structure
2hal is a 2 chain structure with sequence from Hepatitis a virus. Full crystallographic information is available from OCA.
Reference
- Yin J, Cherney MM, Bergmann EM, Zhang J, Huitema C, Pettersson H, Eltis LD, Vederas JC, James MN. An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors. J Mol Biol. 2006 Aug 25;361(4):673-86. Epub 2006 Jul 7. PMID:16860823 doi:10.1016/j.jmb.2006.06.047
- Yin J, Bergmann EM, Cherney MM, Lall MS, Jain RP, Vederas JC, James MN. Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site. J Mol Biol. 2005 Dec 9;354(4):854-71. Epub 2005 Oct 14. PMID:16288920 doi:10.1016/j.jmb.2005.09.074
- Bergmann EM, Cherney MM, Mckendrick J, Frormann S, Luo C, Malcolm BA, Vederas JC, James MN. Crystal structure of an inhibitor complex of the 3C proteinase from hepatitis A virus (HAV) and implications for the polyprotein processing in HAV. Virology. 1999 Dec 5;265(1):153-63. PMID:10603326 doi:10.1006/viro.1999.9968
- Bergmann EM, Mosimann SC, Chernaia MM, Malcolm BA, James MN. The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J Virol. 1997 Mar;71(3):2436-48. PMID:9032381
