Library screening by fragment-based docking.
- Huang D Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
- Caflisch A
- 2009-09-01
Published in:
- Journal of molecular recognition : JMR. - 2010
Amyloid Precursor Protein Secretases
Cathepsin B
Cyclin-Dependent Kinase 2
Enzyme Inhibitors
Enzymes
High-Throughput Screening Assays
Humans
Models, Molecular
Molecular Structure
Peptide Fragments
Peptide Library
Protein Conformation
Protozoan Proteins
RNA Helicases
Receptor, EphB4
Serine Endopeptidases
Viral Nonstructural Proteins
English
We review our computational tools for high-throughput screening by fragment-based docking of large collections of small molecules. Applications to six different enzymes, four proteases, and two protein kinases, are presented. Remarkably, several low-micromolar inhibitors were discovered in each of the high-throughput docking campaigns. Probable reasons for the lack of submicromolar inhibitors are the tiny fraction of chemical space covered by the libraries of available compounds, as well as the approximations in the methods employed for scoring, and the use of a rigid conformation of the target protein.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1002/jmr.981
- PMID 19718684
- Persistent URL
- https://sonar.ch/global/documents/219523
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