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Titolo:
Structure of the pore-farming transmembrane domain of a ligand-gated ion channel
Autore:
Methot, N; Ritchie, BD; Blanton, MP; Baenziger, JE;
Indirizzi:
Univ Ottawa, Dept Biochem Microbiol & Immunol, Ottawa, ON K1H 8M5, Canada Univ Ottawa Ottawa ON Canada K1H 8M5 Immunol, Ottawa, ON K1H 8M5, Canada Texas Tech Univ, Hlth Sci Ctr, Dept Anesthesiol, Lubbock, TX 79430 USA Texas Tech Univ Lubbock TX USA 79430 t Anesthesiol, Lubbock, TX 79430 USA Texas Tech Univ, Hlth Sci Ctr, Dept Pharmacol, Lubbock, TX 79430 USA TexasTech Univ Lubbock TX USA 79430 ept Pharmacol, Lubbock, TX 79430 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 26, volume: 276, anno: 2001,
pagine: 23726 - 23732
SICI:
0021-9258(20010629)276:26<23726:SOTPTD>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
NICOTINIC ACETYLCHOLINE-RECEPTOR; TRANSFORM INFRARED-SPECTROSCOPY; EXCHANGE-RESISTANT CORE; SECONDARY STRUCTURE; TORPEDO-CALIFORNICA; ALPHA-SUBUNIT; SPATIAL STRUCTURE; GLYCINE RECEPTOR; GAMMA-SUBUNIT; PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Baenziger, JE Univ Ottawa, Dept Biochem Microbiol & Immunol, 451 Smyth Rd,Ottawa, ON K1H 8M5, Canada Univ Ottawa 451 Smyth Rd Ottawa ON Canada K1H 8M5 M5, Canada
Citazione:
N. Methot et al., "Structure of the pore-farming transmembrane domain of a ligand-gated ion channel", J BIOL CHEM, 276(26), 2001, pp. 23726-23732

Abstract

The structure of the pore-forming transmembrane domain of the nicotinic acetylcholine receptor from Torpedo has been investigated by infrared spectroscopy. Treatment of affinity-purified receptor with either Pronase or proteinase K digests the extramembranous domains (roughly 75% of the protein mass), leaving hydrophobic membrane-imbedded peptides 3-6 kDa in size that areresistant to peptide H-1/H-2 exchange, Infrared spectra of the transmembrane domain preparations exhibit relatively sharp and symmetric amide I and amide II band contours centered near 1655 and 1545 cm(-1) respectively, in both (H2O)-H-1 and (H2O)-H-2. The amide I band is very similar to the amide I bands observed in the spectra of alpha -helical proteins, such as myoglobin and bacteriorhodopsin, that lack P structure and exhibit much less p-sheet character than is observed in proteins with as little as 20% P sheet. Curve-fitting estimates 75-80% cy-helical character, with the remaining peptides likely adopting extended and/or turn structures at the bilayer surface. Infrared dichroism spectra are consistent with transmembrane alpha -helices oriented perpendicular to the bilayer surface. The evidence strongly suggests that the transmembrane domain of the nicotinic receptor, the most intensively studied ligand-gated ion channel, is composed of five bundles of four transmembrane oi-helices.

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Documento generato il 04/12/20 alle ore 13:10:38