Sensitivity of molecular docking to induced fit effects in influenza virus neuraminidase
- 1 January 2002
- journal article
- Published by Springer Nature in Journal of Computer-Aided Molecular Design
- Vol. 16 (12), 855-869
- https://doi.org/10.1023/a:1023844626572
Abstract
Many proteins undergo small side chain or even backbone movements on binding of different ligands into the same protein structure. This is known as induced fit and is potentially problematic for...Keywords
This publication has 38 references indexed in Scilit:
- A review of protein-small molecule docking methodsJournal of Computer-Aided Molecular Design, 2002
- Analysis of inhibitor binding in influenza virus neuraminidaseProtein Science, 2001
- The Protein Data BankNucleic Acids Research, 2000
- Screening a peptidyl database for potential ligands to proteins with side-chain flexibility.1998
- Design and Synthesis of a Series of Potent and Orally Bioavailable Noncovalent Thrombin Inhibitors That Utilize Nonbasic Groups in the P1 PositionJournal of Medicinal Chemistry, 1998
- Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidaseStructure, 1998
- ‘Flu’ and structure-based drug designStructure, 1997
- Three-dimensional Structure of Influenza A N9 Neuraminidase and Its Complex with the Inhibitor 2-Deoxy 2,3-Dehydro-N-Acetyl Neuraminic AcidJournal of Molecular Biology, 1993
- The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptorProteins-Structure Function and Bioinformatics, 1992
- The neuraminidase of influenza virusProteins-Structure Function and Bioinformatics, 1989