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Titolo:
Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment
Autore:
Horenstein, J; Wagner, DA; Czajkowski, C; Akabas, MH;
Indirizzi:
Yeshiva Univ Albert Einstein Coll Med, Dept Physiol & Biophys, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med, Dept Neurosci, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA Columbia Univ, Dept Physiol, New York, NY 10032 USA Columbia Univ New York NY USA 10032 Dept Physiol, New York, NY 10032 USA Univ Wisconsin, Dept Physiol, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 , Dept Physiol, Madison, WI 53706 USA
Titolo Testata:
NATURE NEUROSCIENCE
fascicolo: 5, volume: 4, anno: 2001,
pagine: 477 - 485
SICI:
1097-6256(200105)4:5<477:PMAGCC>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
GATED ION-CHANNEL; ZN2+ BINDING-SITE; ACETYLCHOLINE-RECEPTOR; BETA-SUBUNIT; POINT MUTATIONS; ALPHA-SUBUNIT; A RECEPTORS; IDENTIFICATION; STOICHIOMETRY; AFFINITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Akabas, MH Yeshiva Univ Albert Einstein Coll Med, Dept Physiol & Biophys, 1300 MorrisPk Ave, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med 1300 Morris Pk Ave Bronx NY USA 10461
Citazione:
J. Horenstein et al., "Protein mobility and GABA-induced conformational changes in GABA(A) receptor pore-lining M2 segment", NAT NEUROSC, 4(5), 2001, pp. 477-485

Abstract

Protein movements underlying ligand-gated ion channel activation are poorly understood. Here we used disulfide bond trapping to examine the proximityand mobility of cysteines substituted for aligned GABA(A) receptor alpha (1) and beta (1) M2 segment channel-lining residues in resting and activatedreceptors. With or without GABA, disulfide bonds formed at alpha (1)N275C/beta (1)E270C (20') and alpha (1)S272C/beta (1)H267C (17'), near the extracellular end, suggesting that this end is more mobile and/or flexible than the rest of the segment. Near the middle of M2, at alpha (1)T261C/beta (1)T256C (6'), a disulfide bond formed only in the presence of GABA and locked the channels open. Channel activation must involve an asymmetric rotation oftwo adjacent subunits toward each other. This would move aligned engineered cysteines on different subunits into proximity and allow disulfide bond formation without blocking conduction. Asymmetric rotation of M2 segments isprobably a common gating mechanism in other ligand-gated ion channels.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/01/20 alle ore 16:07:23