Structural highlights
Function
Q99AU2_9HEPC
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A novel class of non-nucleoside HCV NS5B polymerase inhibitors has been identified from screening. A co-crystal structure revealed an allosteric binding site in the protein that required a unique conformational change to accommodate inhibitor binding. Herein we report the structure-activity relationships (SARs) of this novel class of dihydropyrone-containing compounds that show potent inhibitory activities against the HCV RNA polymerase in biochemical assays.
Identification and structure-based optimization of novel dihydropyrones as potent HCV RNA polymerase inhibitors.,Li H, Tatlock J, Linton A, Gonzalez J, Borchardt A, Dragovich P, Jewell T, Prins T, Zhou R, Blazel J, Parge H, Love R, Hickey M, Doan C, Shi S, Duggal R, Lewis C, Fuhrman S Bioorg Med Chem Lett. 2006 Sep 15;16(18):4834-8. Epub 2006 Jul 7. PMID:16824756[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li H, Tatlock J, Linton A, Gonzalez J, Borchardt A, Dragovich P, Jewell T, Prins T, Zhou R, Blazel J, Parge H, Love R, Hickey M, Doan C, Shi S, Duggal R, Lewis C, Fuhrman S. Identification and structure-based optimization of novel dihydropyrones as potent HCV RNA polymerase inhibitors. Bioorg Med Chem Lett. 2006 Sep 15;16(18):4834-8. Epub 2006 Jul 7. PMID:16824756 doi:10.1016/j.bmcl.2006.06.065
