Quantitative Structure-Activity Relationship Analysis of the Cation Permeability of the P2X2 Channel
| Autor: | Peter P. Mager, Peter Illes, Anje Weber |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Octanol Quantitative structure–activity relationship Protein Conformation Receptors Purinergic P2 Stereochemistry Hydrogen bond Chemistry Molecular Sequence Data Quantitative Structure-Activity Relationship Ion Channels Permeability Rats Structure-Activity Relationship chemistry.chemical_compound Protein structure Permeability (electromagnetism) Cations Drug Discovery Biophysics Extracellular Animals Structure–activity relationship Equilibrium constant Receptors Purinergic P2X2 |
| Zdroj: | Medicinal Chemistry. 1:109-115 |
| ISSN: | 1573-4064 |
| Popis: | The membrane-embedded, ligand-gated P2X glycoprotein receptor is a monovalent-bivalent cation channel that is activated by physiological concentrations of extracellular ATP. A quantitative structure-activity relationship (QSAR) analysis was developed to model the cation permeability of the P2X2 channel and its mutants. As chemical properties, the helix-coil equilibrium constants and the distribution coefficients of the system octanol/water at pH 7.4 were applied and modified (sliding windows) according to Eroshkin et al. (Comput. Appl. Biosci., 1995, 11, 49-44). The results were visualized by a dimeric P2X2 channel construct. The results support the hypothesis that residues which put into the cavity and contribute to hydrogen bonding forces are involved to a control of the transport of hydrated cations through the P2X2 channel. The model may be useful to develop P2X2 receptor antagonists. |
| Databáze: | OpenAIRE |
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