The surface accessibility of the glycine receptor M2-M3 loop is increased in the channel open state

Lynch, J. W., Han, N. L. R., Haddrill, J., Pierce, K. D. and Schofield, P. R. (2001) The surface accessibility of the glycine receptor M2-M3 loop is increased in the channel open state. Journal of Neuroscience, 21 8: 2589-2599.

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Author Lynch, J. W.
Han, N. L. R.
Haddrill, J.
Pierce, K. D.
Schofield, P. R.
Title The surface accessibility of the glycine receptor M2-M3 loop is increased in the channel open state
Journal name Journal of Neuroscience   Check publisher's open access policy
ISSN 0270-6474
Publication date 2001
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 21
Issue 8
Start page 2589
End page 2599
Total pages 11
Editor David C Van Essen
Place of publication USA
Publisher Society for Neuroscience
Collection year 2001
Language eng
Subject C1
320100 Medicine - General
780105 Biological sciences
Abstract Mutations in the extracellular M2-M3 loop of the glycine receptor (GlyR) alpha1 subunit have been shown previously to affect channel gating. In this study, the substituted cysteine accessibility method was used to investigate whether a structural rearrangement of the M2-M3 loop accompanies GlyR activation. All residues from R271C to V277C were covalently modified by both positively charged methanethiosulfonate ethyltrimethylammonium (MTSET) and negatively charged methanethiosulfonate ethylsulfonate (MTSES), implying that these residues form an irregular surface loop. The MTSET modification rate of all residues from R271C to K276C was faster in the glycine-bound state than in the unliganded state. MTSES modification of A272C, L274C, and V277C was also faster in the glycine-bound state. These results demonstrate that the surface accessibility of the M2-M3 loop is increased as the channel transitions from the closed to the open state, implying that either the loop itself or an overlying domain moves during channel activation.
Keyword Neurosciences
Ligand-gated Ion Channel
Glycine Receptor Alpha 1 Subunit
Substituted Cysteine Accessibility Method (scam)
Methanethiosulfonate Ethyltrimethlammonium (mtset)
Methanethiosulfonate Ethylsulfonate (mtses)
Hyperekplexia
Neuronal Nicotinic Receptors
Membrane-spanning Segment
Acetylcholine-receptor
Gaba(a) Receptor
M2 Segment
Sporadic Hyperekplexia
Alpha-subunit
Binding-sites
Mutation
Identification
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biomedical Sciences Publications
 
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Created: Tue, 14 Aug 2007, 16:50:06 EST