2p59

Crystal Structure of Hepatitis C Virus NS3.4A protease

spinqualitylabelsall models 2p59, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2p59 is a 4 chain structure with sequence from Hepacivirus hominis and Hepatitis C virus (isolate H). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: GG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q91RS4_9HEPC Publication Abstract from PubMed 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. Inhibitors of hepatitis C virus NS3.4A protease. Effect of P4 capping groups on inhibitory potency and pharmacokinetics.,Perni RB, Chandorkar G, Cottrell KM, Gates CA, Lin C, Lin K, Luong YP, Maxwell JP, Murcko MA, Pitlik J, Rao G, Schairer WC, Van Drie J, Wei Y Bioorg Med Chem Lett. 2007 Jun 15;17(12):3406-11. Epub 2007 Apr 3. PMID:17482818 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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