1w3c | pdb_00001w3c
From Proteopedia
CRYSTAL STRUCTURE OF THE HEPATITIS C VIRUS NS3 PROTEASE IN COMPLEX WITH A PEPTIDOMIMETIC INHIBITOR
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe design of a series of peptidomimetic inhibitors of the hepatitis C virus NS3 protease is described. These inhibitors feature an indoline-2-carboxamide as a novel heterocyclic replacement for the P3 amino acid residue and N-terminal capping group of tripeptide based inhibitors. The crystal structure of the ternary NS3/NS4A/inhibitor complex for the most active molecule in this series highlights its suitability as an N-terminal capping group of a dipeptide inhibitor of the NS3 protease. The design and enzyme-bound crystal structure of indoline based peptidomimetic inhibitors of hepatitis C virus NS3 protease.,Ontoria JM, Di Marco S, Conte I, Di Francesco ME, Gardelli C, Koch U, Matassa VG, Poma M, Steinkuhler C, Volpari C, Harper S J Med Chem. 2004 Dec 16;47(26):6443-6. PMID:15588076[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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