2o5d | pdb_00002o5d
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Thiazolone-acylsulfonamides as novel HCV NS5B polymerase allosteric inhibitors: Convergence of structure-based drug design and X-ray crystallographic study
Overview
A novel series of thiazolone-acylsulfonamides were designed as HCV NS5B, polymerase allosteric inhibitors. The structure based drug designs (SBDD), were guided by docking results that revealed the potential to explore an, additional pocket in the allosteric site. In particular, the designed, molecules contain moieties of previously described thiazolone and a newly, designed acylsulfonamide linker that is in turn connected with a, substituted aromatic ring. The selected compounds were synthesized and, demonstrated low muM activity. The X-ray complex structure was determined, at a 2.2A resolution and converged with the SBDD principle.
About this Structure
2O5D is a Protein complex structure of sequences from Hepatitis c virus with VR1 as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
Reference
Thiazolone-acylsulfonamides as novel HCV NS5B polymerase allosteric inhibitors: Convergence of structure-based drug design and X-ray crystallographic study., Yan S, Appleby T, Larson G, Wu JZ, Hamatake RK, Hong Z, Yao N, Bioorg Med Chem Lett. 2007 Jan 19;. PMID:17276060
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