Solid-State NMR for the analysis of high affinity ligand/receptor interactions
Solid-State NMR for the analysis of high affinity ligand/receptor interactions
The rational development of drugs which target integral membrane proteins relies intimately on our understanding of their interactions with their binding sites. Advances in solid-state NMR methodology coupled to improved expression and purification strategies for membrane proteins now enable us to probe the structure, dynamics, and binding modes of these drugs with ever-increasing resolution. This article seeks to highlight these advances demonstrating how improvements in protein expression and purification can be coupled with recent developments in instrumentation and pulse sequences in magic-angle spinning, static, and oriented sample solid-state NMR to reveal structural and dynamic information of high-affinity drugs/ligands within their binding sites on membrane proteins. Furthermore, we will highlight some of the major experimental considerations associated with performing these studies
membrane proteins, magic-angle spinning, dipolar recoupling, oriented samples, rational drug design, pharmacology, ligands, small molecules, receptors
144-172
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
May 2009
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Williamson, P.T.F.
(2009)
Solid-State NMR for the analysis of high affinity ligand/receptor interactions.
Concepts in Magnetic Resonance Part A, 34A (3), .
(doi:10.1002/cmr.a.20140).
Abstract
The rational development of drugs which target integral membrane proteins relies intimately on our understanding of their interactions with their binding sites. Advances in solid-state NMR methodology coupled to improved expression and purification strategies for membrane proteins now enable us to probe the structure, dynamics, and binding modes of these drugs with ever-increasing resolution. This article seeks to highlight these advances demonstrating how improvements in protein expression and purification can be coupled with recent developments in instrumentation and pulse sequences in magic-angle spinning, static, and oriented sample solid-state NMR to reveal structural and dynamic information of high-affinity drugs/ligands within their binding sites on membrane proteins. Furthermore, we will highlight some of the major experimental considerations associated with performing these studies
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Published date: May 2009
Keywords:
membrane proteins, magic-angle spinning, dipolar recoupling, oriented samples, rational drug design, pharmacology, ligands, small molecules, receptors
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Local EPrints ID: 72082
URI: http://eprints.soton.ac.uk/id/eprint/72082
ISSN: 1546-6086
PURE UUID: 12df2316-31a1-4d91-a16b-1076eae1d495
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Date deposited: 20 Jan 2010
Last modified: 14 Mar 2024 02:52
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