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Titolo:
Tertiary interactions between the fifth and sixth transmembrane segments of rhodopsin
Autore:
Struthers, M; Yu, HB; Kono, M; Oprian, DD;
Indirizzi:
Brandeis Univ, Dept Biochem, Waltham, MA 02454 USA Brandeis Univ Waltham MA USA 02454 v, Dept Biochem, Waltham, MA 02454 USA Brandeis Univ, Volen Ctr Complex Syst, Waltham, MA 02454 USA Brandeis Univ Waltham MA USA 02454 tr Complex Syst, Waltham, MA 02454 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 20, volume: 38, anno: 1999,
pagine: 6597 - 6603
SICI:
0006-2960(19990518)38:20<6597:TIBTFA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-COUPLED RECEPTORS; TACHYKININ NK-1 RECEPTOR; DISULFIDE CROSS-LINKING; MONOCLONAL-ANTIBODIES; TRANSDUCIN ACTIVATION; ASPARTATE RECEPTOR; BOVINE RHODOPSIN; BINDING-SITES; HELICES; ARRANGEMENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Oprian, DD Brandeis Univ, Dept Biochem, Waltham, MA 02454 USA Brandeis Univ Waltham MA USA 02454 chem, Waltham, MA 02454 USA
Citazione:
M. Struthers et al., "Tertiary interactions between the fifth and sixth transmembrane segments of rhodopsin", BIOCHEM, 38(20), 1999, pp. 6597-6603

Abstract

We have used cysteine scanning mutagenesis and disulfide cross-linking in a split rhodopsin construct to investigate the secondary structure and tertiary contacts of the fifth (TM5) and sixth (TM6) transmembrane segments of rhodopsin, Using a simple increase in pH to promote disulfide bond formation, three cross-links between residues on the extracellular side of TM5 (at positions 198, 200, and 204) and TM6 (at position 276) have been identifiedand characterized. The helical pattern of cross-linking observed indicatesthat the fifth transmembrane helix extends through residue 200 but does not include residue 198. Rhodopsin mutants containing these disulfides demonstrate nativelike absorption spectra and light-dependent activation of transducin, suggesting that large movements on the extracellular side of TM5 with respect to TM6 are not required for receptor activation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 00:53:25