Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114
- 4 August 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 363 (1) , 161-173
- https://doi.org/10.1016/j.jmb.2006.08.007
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 Å resolution crystal structures of HIV‐1 protease mutants with substrate analogsThe FEBS Journal, 2005
- Beta-lactam compounds as apparently uncompetitive inhibitors of HIV-1 proteaseBioorganic & Medicinal Chemistry Letters, 2005
- High Resolution Crystal Structures of HIV-1 Protease with a Potent Non-peptide Inhibitor (UIC-94017) Active Against Multi-drug-resistant Clinical StrainsJournal of Molecular Biology, 2004
- Crystal structures of HIV protease V82A and L90M mutants reveal changes in the indinavir‐binding siteEuropean Journal of Biochemistry, 2004
- The Mechanism of γ-SecretasePublished by Elsevier ,2003
- Structural and kinetic analysis of drug resistant mutants of HIV‐1 proteaseEuropean Journal of Biochemistry, 1999
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- Inhibition of porcine pepsin by two substrate analogs containing statine. The effect of histidine at the P2 subsite on the inhibition of aspartic proteinasesJournal of Medicinal Chemistry, 1988