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Titolo:
The surface accessibility of the glycine receptor M2-M3 loop is increased in the channel open state
Autore:
Lynch, JW; Han, NLR; Haddrill, J; Pierce, KD; Schofield, PR;
Indirizzi:
Univ Queensland, Dept Physiol & Pharmacol, Brisbane, Qld 4072, Australia Univ Queensland Brisbane Qld Australia 4072 Brisbane, Qld 4072, Australia Garvan Inst Med Res, Neurobiol Program, Sydney, NSW 2010, Australia GarvanInst Med Res Sydney NSW Australia 2010 Sydney, NSW 2010, Australia
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 8, volume: 21, anno: 2001,
pagine: 2589 - 2599
SICI:
0270-6474(20010415)21:8<2589:TSAOTG>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEURONAL NICOTINIC RECEPTORS; MEMBRANE-SPANNING SEGMENT; ACETYLCHOLINE-RECEPTOR; GABA(A) RECEPTOR; M2 SEGMENT; SPORADIC HYPEREKPLEXIA; ALPHA-SUBUNIT; BINDING-SITES; MUTATION; IDENTIFICATION;
Keywords:
ligand-gated ion channel; glycine receptor alpha 1 subunit; substituted cysteine accessibility method (SCAM); methanethiosulfonate ethyltrimethlammonium (MTSET); methanethiosulfonate ethylsulfonate (MTSES); hyperekplexia;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Lynch, JW Univ Queensland, Dept Physiol & Pharmacol, Brisbane, Qld 4072, Australia Univ Queensland Brisbane Qld Australia 4072 Qld 4072, Australia
Citazione:
J.W. Lynch et al., "The surface accessibility of the glycine receptor M2-M3 loop is increased in the channel open state", J NEUROSC, 21(8), 2001, pp. 2589-2599

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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 21:15:36