Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The 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 Also
References
- ↑ Ontoria JM, Di Marco S, Conte I, Di Francesco ME, Gardelli C, Koch U, Matassa VG, Poma M, Steinkuhler C, Volpari C, Harper S. The design and enzyme-bound crystal structure of indoline based peptidomimetic inhibitors of hepatitis C virus NS3 protease. J Med Chem. 2004 Dec 16;47(26):6443-6. PMID:15588076 doi:10.1021/jm049435d
