Binding site analysis of full-length α1a adrenergic receptor using homology modeling and molecular docking
- 1 June 2004
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 319 (2) , 493-500
- https://doi.org/10.1016/j.bbrc.2004.04.149
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties11Edited by B. HonigJournal of Molecular Biology, 2001
- Non-α-helical elements modulate polytopic membrane protein architecture11Edited by G. Von HeijneJournal of Molecular Biology, 2001
- Crystal Structure of Rhodopsin: A G Protein-Coupled ReceptorScience, 2000
- Novel Aromatic Residues in Transmembrane Domains IV and V Involved in Agonist Binding at α1a-Adrenergic ReceptorsJournal of Biological Chemistry, 2000
- ??-Adrenoceptor Antagonists in the Treatment of Benign Prostatic HyperplasiaDrugs, 1999
- An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- Geometry of proline‐containing alpha‐helices in proteinsInternational Journal of Peptide and Protein Research, 1992
- Assessment of protein models with three-dimensional profilesNature, 1992
- Receptor interaction for the α-antagonist WB4101 (2-(N[2,6-dimethyoxyphenoxyethyl])amino-methyl-1,4-benzodioxane)Journal of Pharmacy and Pharmacology, 1978