NMR of drugs and ligands bound to membrane receptors.

NMR methods are now able to give detailed structural, dynamic and electronic information about drugs and ligands while constrained at their site of action in membrane-embedded receptors, information which is essential for mechanistic descriptions of their action and design of new ligands. Using soli...

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Autor principal: Watts, A
Formato: Journal article
Lenguaje:English
Publicado: 1999
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author Watts, A
author_facet Watts, A
author_sort Watts, A
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description NMR methods are now able to give detailed structural, dynamic and electronic information about drugs and ligands while constrained at their site of action in membrane-embedded receptors, information which is essential for mechanistic descriptions of their action and design of new ligands. Using solid state NMR methods, a peptic ulcer drug analogue has been described at atomic resolution (to +/- 0.3 A between two atoms) at its site of action in the gastric H+/K+-ATPase, and the aromaticity of the agonist binding site of the nicotinic acetylcholine receptor has been demonstrated, with both targets in functionally competent membranes under conditions similar to those used in screening assays. G-protein-coupled receptor ligands and prosthetic groups are also being resolved using NMR methods.
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spelling oxford-uuid:476154b1-e351-47a3-9d66-682da7062bcd2022-03-26T15:19:50ZNMR of drugs and ligands bound to membrane receptors.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:476154b1-e351-47a3-9d66-682da7062bcdEnglishSymplectic Elements at Oxford1999Watts, ANMR methods are now able to give detailed structural, dynamic and electronic information about drugs and ligands while constrained at their site of action in membrane-embedded receptors, information which is essential for mechanistic descriptions of their action and design of new ligands. Using solid state NMR methods, a peptic ulcer drug analogue has been described at atomic resolution (to +/- 0.3 A between two atoms) at its site of action in the gastric H+/K+-ATPase, and the aromaticity of the agonist binding site of the nicotinic acetylcholine receptor has been demonstrated, with both targets in functionally competent membranes under conditions similar to those used in screening assays. G-protein-coupled receptor ligands and prosthetic groups are also being resolved using NMR methods.
spellingShingle Watts, A
NMR of drugs and ligands bound to membrane receptors.
title NMR of drugs and ligands bound to membrane receptors.
title_full NMR of drugs and ligands bound to membrane receptors.
title_fullStr NMR of drugs and ligands bound to membrane receptors.
title_full_unstemmed NMR of drugs and ligands bound to membrane receptors.
title_short NMR of drugs and ligands bound to membrane receptors.
title_sort nmr of drugs and ligands bound to membrane receptors
work_keys_str_mv AT wattsa nmrofdrugsandligandsboundtomembranereceptors