Exploring ligand recognition and ion flow in comparative models of the human GABA type A receptor
| Autor: | S.L. Chan, Vassiliy N. Bavro, Kenji Mizuguchi, Ian L. Martin, N.P. Todorov, Younes Mokrab, P.-L. Chau, Susan M. J. Dunn |
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| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Molecular Sequence Data Flunitrazepam Ligands Protein Structure Secondary GABAA-rho receptor chemistry.chemical_compound Benzodiazepines GABA receptor Muscarinic acetylcholine receptor M5 Materials Chemistry Humans Computer Simulation Amino Acid Sequence Physical and Theoretical Chemistry Receptor Spectroscopy gamma-Aminobutyric Acid Binding Sites Sequence Homology Amino Acid GABAA receptor Muscimol Receptors GABA-A Computer Graphics and Computer-Aided Design Protein Structure Tertiary Nicotinic acetylcholine receptor chemistry Biochemistry Biophysics Alpha-4 beta-2 nicotinic receptor Ion Channel Gating |
| Zdroj: | Journal of molecular graphics and modelling. 26(4) |
| ISSN: | 1873-4243 1093-3263 |
| Popis: | We present two comparative models of the GABAA receptor. Model 1 is based on the 4-A resolution structure of the nicotinic acetylcholine receptor from Torpedo marmorata and represents the unliganded receptor. Two agonists, GABA and muscimol, two benzodiazepines, flunitrazepam and alprazolam, together with the general anaesthetic halothane, have been docked to this model. The ion flow is also explored in model 1 by evaluating the interaction energy of a chloride ion as it traverses the extracellular, transmembrane and intracellular domains of the protein. Model 2 differs from model 1 only in the extracellular domain and represents the liganded receptor. Comparison between the two models not only allows us to explore commonalities and differences with comparative models of the nicotinic acetylcholine receptor, but also suggests possible protein sub-domain interactions with the GABAA receptor not previously addressed. |
| Databáze: | OpenAIRE |
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