1DXP
Inhibition of the Hepatitis C Virus NS3/4A Protease. The Crystal Structures of Two Protease-Inhibitor Complexes (apo structure)
Summary for 1DXP
| Entry DOI | 10.2210/pdb1dxp/pdb |
| Related | 1DY8 1DY9 1JXP |
| Descriptor | PROTEASE/HELICASE NS3 (P70), NONSTRUCTURAL PROTEIN NS4A (P4), ZINC ION, ... (5 entities in total) |
| Functional Keywords | serine protease, ns3, ns4a, hepatitis c virus, protease inhibition, hydrolase |
| Biological source | HEPATITIS C VIRUS (ISOLATE TAIWAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 43094.21 |
| Authors | Di Marco, S.,Rizzi, M.,Volpari, C.,Walsh, M.,Narjes, F.,Colarusso, S.,De Francesco, R.,Matassa, V.G.,Sollazzo, M. (deposition date: 2000-01-13, release date: 2001-01-12, Last modification date: 2023-12-06) |
| Primary citation | Di Marco, S.,Rizzi, M.,Volpari, C.,Walsh, M.,Narjes, F.,Colarusso, S.,De Francesco, R.,Matassa, V.G.,Sollazzo, M. Inhibition of the Hepatitis C Virus Ns3/4A Protease the Crystal Structures of Two Protease-Inhibitor Complexes J.Biol.Chem., 275:7152-, 2000 Cited by PubMed Abstract: The hepatitis C virus NS3 protein contains a serine protease domain with a chymotrypsin-like fold, which is a target for development of therapeutics. We report the crystal structures of this domain complexed with NS4A cofactor and with two potent, reversible covalent inhibitors spanning the P1-P4 residues. Both inhibitors bind in an extended backbone conformation, forming an anti-parallel beta-sheet with one enzyme beta-strand. The P1 residue contributes most to the binding energy, whereas P2-P4 side chains are partially solvent exposed. The structures do not show notable rearrangements of the active site upon inhibitor binding. These results are significant for the development of antivirals. PubMed: 10702283DOI: 10.1074/JBC.275.10.7152 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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