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Structure-based discovery of [[beta].sub.2]-adrenergic receptor ligands
- Source :
- Proceedings of the National Academy of Sciences of the United States. April 21, 2009, Vol. 106 Issue 16, p6843, 6 p.
- Publication Year :
- 2009
-
Abstract
- Aminergic G protein-coupled receptors (GPCRs) have been a major focus of pharmaceutical research for many years. Due partly to the lack of reliable receptor structures, drug discovery efforts have been largely ligand-based. The recently determined X-ray structure of the [[beta].sub.2]-adrenergic receptor offers an opportunity to investigate the advantages and limitations inherent in a structure-based approach to ligand discovery against this and related GPCR targets. Approximately 1 million commercially available, 'lead-like' molecules were docked against the [[beta].sub.2]-adrenergic receptor structure. On testing of 25 high-ranking molecules, 6 were active with binding affinities docking | GPCR | inverse agonists | library bias | ligand design
Details
- Language :
- English
- ISSN :
- 00278424
- Volume :
- 106
- Issue :
- 16
- Database :
- Gale General OneFile
- Journal :
- Proceedings of the National Academy of Sciences of the United States
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.199396465