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Titolo:
Molecular model of the Escherichia coli Na-1/H-1 antiporter NhaA
Autore:
Ravna, AW; Sylte, I; Dahl, SG;
Indirizzi:
Univ Tromso, Inst Med Biol, Dept Pharmacol, N-9037 Tromso, Norway Univ Tromso Tromso Norway N-9037 , Dept Pharmacol, N-9037 Tromso, Norway
Titolo Testata:
RECEPTORS & CHANNELS
fascicolo: 4, volume: 7, anno: 2001,
pagine: 319 - 328
SICI:
1060-6823(2001)7:4<319:MMOTEC>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
NA+/H+ ANTIPORTER; TRANSMEMBRANE DOMAIN; TRANSPORT PROTEIN; COCAINE BINDING; PH RESPONSE; DATA-BANK; RESIDUES; MUTAGENESIS; SUBSTRATE; AMILORIDE;
Keywords:
Na+/H+ antiporter; molecular structure; molecular dynamics; 3D-model;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Sylte, I Univ Tromso, Inst Med Biol, Dept Pharmacol, N-9037 Tromso, NorwayUniv Tromso Tromso Norway N-9037 armacol, N-9037 Tromso, Norway
Citazione:
A.W. Ravna et al., "Molecular model of the Escherichia coli Na-1/H-1 antiporter NhaA", RECEPT CHAN, 7(4), 2001, pp. 319-328

Abstract

A three-dimensional electron density projection map of the ion-coupled membrane protein Escherichia coli Na+/H+ antiporter (NhaA) was recently published. Based on this projection map, and previous biophysical studies determining the assignment of the 12 transmembrane a-helices (TMHs), a three-dimensional molecular model of the NhaA was constructed, using interactive molecular graphics and energy calculations. The diuretic drug, amiloride, was docked into the model and putative interacting amino acids were identified. The model suggests that the pH dependent activity of NhaA may be explained by charge changes in the intracellular loop between TMH8 and TMH9 which alter the positions of TMHs 4, 5 and 11 relative to each other, such that a pore area of the transporter protein is opened.

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Documento generato il 25/11/20 alle ore 18:58:35