2P59
Crystal Structure of Hepatitis C Virus NS3.4A protease
Summary for 2P59
| Entry DOI | 10.2210/pdb2p59/pdb |
| Descriptor | NS3, peptide, (2S,3AS,7AS)-1-[(2S)-2-{[(2S)-2-CYCLOHEXYL-2-({[(2R)-4-NITRO-2H-PYRROL-2-YL]CARBONYL}AMINO)ACETYL]AMINO}-3,3-DIMETHYLBUTANOYL]-N-{(1S)-1-[(1R)-2-(CYCLOPROPYLAMINO)-1-HYDROXY-2-OXOETHYL]BUTYL}OCTAHYDRO-1H-INDOLE-2-CARBOXAMIDE (3 entities in total) |
| Functional Keywords | hcv protease, viral protein |
| Biological source | Hepatitis C virus More |
| Total number of polymer chains | 4 |
| Total formula weight | 43242.94 |
| Authors | Perni, R.B.,Wei, Y. (deposition date: 2007-03-14, release date: 2008-02-05, Last modification date: 2024-11-06) |
| Primary citation | Perni, R.B.,Chandorkar, G.,Cottrell, K.M.,Gates, C.A.,Lin, C.,Lin, K.,Luong, Y.P.,Maxwell, J.P.,Murcko, M.A.,Pitlik, J.,Rao, G.,Schairer, W.C.,Van Drie, J.,Wei, Y. Inhibitors of hepatitis C virus NS3.4A protease. Effect of P4 capping groups on inhibitory potency and pharmacokinetics. Bioorg.Med.Chem.Lett., 17:3406-3411, 2007 Cited by PubMed Abstract: Reversible tetrapeptide-based compounds have been shown to effectively inhibit the hepatitis C virus NS3.4A protease. Inhibition of viral replicon RNA production in Huh-7 cells has also been demonstrated. We show herein that the inclusion of hydrogen bond donors on the P4 capping group of tetrapeptide-based inhibitors result in increased binding potency to the NS3.4A protease. The capping groups also impart significant effects on the pharmacokinetic profile of these inhibitors. PubMed: 17482818DOI: 10.1016/j.bmcl.2007.03.090 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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