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Titolo:
Glycine receptors: What gets in and why?
Autore:
Barry, PH; Schofield, PR; Moorhouse, AJ;
Indirizzi:
Univ New S Wales, Sch Physiol & Pharmacol, Sydney, NSW 2052, Australia Univ New S Wales Sydney NSW Australia 2052 l, Sydney, NSW 2052, Australia Garvan Inst Med Res, Sydney, NSW, Australia Garvan Inst Med Res Sydney NSW Australia Med Res, Sydney, NSW, Australia
Titolo Testata:
CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY
fascicolo: 11, volume: 26, anno: 1999,
pagine: 935 - 936
SICI:
0305-1870(199911)26:11<935:GRWGIA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED HIPPOCAMPAL-NEURONS; TRANSMEMBRANE SEGMENT; CHLORIDE CONDUCTANCE; ANION PERMEATION; CHANNEL; LOCATION; RESIDUE;
Keywords:
glycine receptor channel; ion channels; ion permeation; ion selectivity; ligand-gated ion channel superfamily;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
12
Recensione:
Indirizzi per estratti:
Indirizzo: Barry, PH Univ New S Wales, Sch Physiol & Pharmacol, Sydney, NSW 2052, Australia Univ New S Wales Sydney NSW Australia 2052 NSW 2052, Australia
Citazione:
P.H. Barry et al., "Glycine receptors: What gets in and why?", CLIN EXP PH, 26(11), 1999, pp. 935-936

Abstract

1, The glycine receptor channel (GlyR), a member of the ligand-gated ion channel superfamily; shares many similar permeation properties with the GABAA receptor channel.2, The GlyR is anion permeable, with P-K/P-Cl < 0,05, has a 5-6 Angstrom minimum pore diameter and a permeation selectivity sequence dominated by hydration energies.3, The channels, which display multiple subconductance states, can be multiply occupied,4 Two positive arginine rings at the ends of the pore region may contribute to the anion selectivity of the GlyR,5, Mutation of the extracellular charged arginine ring can impair channel function by decreasing the sensitivity of glycine activation, reducing channel conductance, shifting the normal multi-subconductance states to lower values and by decoupling the link between ligand binding and channel gating,6, These and other site-directed mutagenesis studies of recombinant GlyR;RI together with studies of native GlyR, are providing further insights intowhat controls gating and ion permeation and selectivity through this channel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:53:04