Molecular mimicry of substrate oxygen atoms by water molecules in the β-amylase active site
Open Access
- 1 August 2001
- journal article
- Published by Wiley in Protein Science
- Vol. 10 (8) , 1645-1657
- https://doi.org/10.1110/ps.8201
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Anatomy of a conformational transition of β-strand 6 in soybean P-amylase caused by substrate (or inhibitor) binding to the catalytical siteProtein Science, 2008
- Contribution of water molecules in the interior of a protein to the conformational stabilityJournal of Molecular Biology, 1997
- Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearest-neighbors genetic algorithmJournal of Molecular Biology, 1997
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug designChemistry & Biology, 1996
- Satisfying Hydrogen Bonding Potential in ProteinsJournal of Molecular Biology, 1994
- Rational Design of Potent, Bioavailable, Nonpeptide Cyclic Ureas as HIV Protease InhibitorsScience, 1994
- 2.0 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergentActa Crystallographica Section D-Biological Crystallography, 1993
- Mechanism of maltal hydration catalyzed by .beta.-amylase: role of protein structure in controlling the steric outcome of reactions catalyzed by a glycosylaseBiochemistry, 1991
- Design, Activity, and 2.8 Å Crystal Structure of a C 2 Symmetric Inhibitor Complexed to HIV-1 ProteaseScience, 1990