2asg: Difference between revisions
New page: '''Theoretical Model''' The entry 2ASG is a Theoretical Model titled 'Binding Domain of Non-competitive Inhibitors In the alpha3beta4 subtype of nicotinic acetylcholine receptor'. [[Cate... |
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{{Theoretical_model}} | |||
==BINDING DOMAIN OF NON-COMPETITIVE INHIBITORS IN THE ALPHA3BETA4 SUBTYPE OF NICOTINIC ACETYLCHOLINE RECEPTOR== | |||
<StructureSection load='2asg' size='340' side='right'caption='[[2asg]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ASG FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2asg FirstGlance], [https://www.ebi.ac.uk/pdbsum/2asg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2asg ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A large number of drug substances act as noncompetitive inhibitors (NCIs) of the nicotinic acetylcholine receptor (nAChR) by blocking the ion flux through the channel. An affinity chromatography technique has been developed for investigating the interactions between NCIs and the alpha3beta4 subtype of neuronal nAChR. The data obtained from the chromatographic study were used to construct QSAR models of the NCI-nAChR binding with both electronic and steric parameters observed as important descriptors. A molecular model of the transmembrane domain of the alpha3beta4 subtype of nAChR was constructed and used to simulate the docking of a series of NCIs. A key aspect of the model was the discovery of the cleft produced by the incorporation of the bulky phenylalanine moiety into the nonpolar section of the lumen by the beta4 subunit. Quantitatively, the results of docking simulations modeled the experimental affinity data better than QSAR results. The computational approach, combined with the modeling of NCI-nAChR interaction by affinity chromatography, can be used to predict possible toxicities and adverse interactions. | |||
Interaction of noncompetitive inhibitors with an immobilized alpha3beta4 nicotinic acetylcholine receptor investigated by affinity chromatography, quantitative-structure activity relationship analysis, and molecular docking.,Jozwiak K, Ravichandran S, Collins JR, Wainer IW J Med Chem. 2004 Jul 29;47(16):4008-21. PMID:15267239<ref>PMID:15267239</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2asg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Collins, J R]] | |||
[[Category: Jozwiak, K]] | |||
[[Category: Ravichandran, S]] | |||
[[Category: Wainer, I W]] | |||
Latest revision as of 17:44, 17 November 2021
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BINDING DOMAIN OF NON-COMPETITIVE INHIBITORS IN THE ALPHA3BETA4 SUBTYPE OF NICOTINIC ACETYLCHOLINE RECEPTORBINDING DOMAIN OF NON-COMPETITIVE INHIBITORS IN THE ALPHA3BETA4 SUBTYPE OF NICOTINIC ACETYLCHOLINE RECEPTOR
Structural highlights
Publication Abstract from PubMedA large number of drug substances act as noncompetitive inhibitors (NCIs) of the nicotinic acetylcholine receptor (nAChR) by blocking the ion flux through the channel. An affinity chromatography technique has been developed for investigating the interactions between NCIs and the alpha3beta4 subtype of neuronal nAChR. The data obtained from the chromatographic study were used to construct QSAR models of the NCI-nAChR binding with both electronic and steric parameters observed as important descriptors. A molecular model of the transmembrane domain of the alpha3beta4 subtype of nAChR was constructed and used to simulate the docking of a series of NCIs. A key aspect of the model was the discovery of the cleft produced by the incorporation of the bulky phenylalanine moiety into the nonpolar section of the lumen by the beta4 subunit. Quantitatively, the results of docking simulations modeled the experimental affinity data better than QSAR results. The computational approach, combined with the modeling of NCI-nAChR interaction by affinity chromatography, can be used to predict possible toxicities and adverse interactions. Interaction of noncompetitive inhibitors with an immobilized alpha3beta4 nicotinic acetylcholine receptor investigated by affinity chromatography, quantitative-structure activity relationship analysis, and molecular docking.,Jozwiak K, Ravichandran S, Collins JR, Wainer IW J Med Chem. 2004 Jul 29;47(16):4008-21. PMID:15267239[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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