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Titolo:
Solution structures of the cytoplasmic linkers between segments S-4 and S-5 (S-4-S-5) in domains III and IV of human brain sodium channels in SDS micelles
Autore:
Miyamoto, K; Nakagawa, T; Kuroda, Y;
Indirizzi:
Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 aceut Sci, Sakyo Ku, Kyoto 6068501, Japan
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 3, volume: 58, anno: 2001,
pagine: 193 - 203
SICI:
1397-002X(200109)58:3<193:SSOTCL>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
INACTIVATION GATE; SECONDARY STRUCTURE; S4-S5 LINKER; PROTEINS; SPECTRA; SPECTROSCOPY; MUTAGENESIS; MOVEMENT; LOOP;
Keywords:
circular dichroism; H-1 NMR; inactivation gate; sodium channel; SDS micelles; S4-S5 linker; III-IV linker;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Kuroda, Y Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 Sakyo Ku, Kyoto 6068501, Japan
Citazione:
K. Miyamoto et al., "Solution structures of the cytoplasmic linkers between segments S-4 and S-5 (S-4-S-5) in domains III and IV of human brain sodium channels in SDS micelles", J PEPT RES, 58(3), 2001, pp. 193-203

Abstract

The two cytoplasmic linkers connecting segment S4 and segment S5 (S4-S5 linker) of both domain III (III/S4-S5) and IV (IV/S4-S5) of the sodium channel a-subunit are considered to work as a hydrophobic receptor for the inactivation particle because of the three hydrophobic amino acids of Ile-Phe-Met(IFM motif) in the III-IV linker of the sodium channel chi -subunit. To date, the solution structures of the peptides related to III/S4-S5 (MP-D3: A1325-M1338) and IV/S4-S5 (MP-D4: T1648-L1666) of human brain sodium channelshave been investigated using CD and H-1 NMR spectroscopies. SIDS micelles were employed as a solvent. The micelles mimic either biological membranes or the interior of a protein and can be a relevant environment at the inactivated state of the channels. It was found that the secondary structures ofboth MP-D3 and MP-D4 assume chi -helical conformations around the N-terminal half-side of the sequences, i.e. the residues between V1326 and L1331 inMP-D3 and between L1650 and S1656 in MP-D4. Residue A1329 in MP-D3, which is considered to interact with F1489 of the IFM motif, was found to be located within the chi -helix. Residues F1651, M1654, M1655, L1657 and A1669 inMP-D4, which also play an important role in inactivation, formed a hydrophobic cluster on one side of the helix. This cluster was concluded to Dates:interact with the hydrophobic cluster due to the III-IV linker before the inactivation gate closes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 06:33:02