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Titolo:
G-protein-coupled receptors for light: The three-dimensional structure of rhodopsin
Autore:
Essen, LO;
Indirizzi:
Max Planck Inst Biochem, Dept Membrane Biochem, D-82152 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82152 Martinsried, Germany
Titolo Testata:
CHEMBIOCHEM
fascicolo: 7-8, volume: 2, anno: 2001,
pagine: 513 -
SICI:
1439-4227(20010803)2:7-8<513:GRFLTT>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
VISUAL PIGMENT RHODOPSIN; 2.3 ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE; CRYSTALLIZATION; BACTERIORHODOPSIN; MEMBRANES; FRAGMENT; COMPLEX; NMR;
Keywords:
membrane proteins; receptors; rhodopsin; signal transduction; vision;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Essen, LO Max Planck Inst Biochem, Dept Membrane Biochem, Klopferspitz 18A, D-82152 Martinsried, Germany Max Planck Inst Biochem Klopferspitz 18A Martinsried Germany D-82152
Citazione:
L.O. Essen, "G-protein-coupled receptors for light: The three-dimensional structure of rhodopsin", CHEMBIOCHEM, 2(7-8), 2001, pp. 513

Abstract

Two decades of structural studies on visual pigments culminated recently in the first crystal structure of bovine rhodopsin (see picture). In this archetypal G-protein-coupled receptor (GPCR) the sites of signal input, the retinal-binding site, and signal output, the G-protein-binding site, are separated by more than 40 Angstrom. Using a multitude of biophysical and biochemical approaches, researchers now attempt to delineate a common mechanism by which signal transmission occurs in GPCRs. Furthermore, molecular details of the retinal-binding site yield first clues as to how color tuning is performed in visual pigments.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 23:55:14