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Titolo:
Functional role of tryptophan residues in the fourth transmembrane domain of the CB2 cannabinoid receptor
Autore:
Rhee, MH; Nevo, I; Bayewitch, ML; Zagoory, O; Vogel, Z;
Indirizzi:
Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 biol, IL-76100 Rehovot, Israel
Titolo Testata:
JOURNAL OF NEUROCHEMISTRY
fascicolo: 6, volume: 75, anno: 2000,
pagine: 2485 - 2491
SICI:
0022-3042(200012)75:6<2485:FROTRI>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-COUPLED RECEPTORS; SITE-DIRECTED MUTAGENESIS; TACHYKININ NK2 RECEPTOR; ADENYLYL-CYCLASE; SEQUENCE ALIGNMENT; AROMATIC RESIDUES; LYSINE RESIDUE; BINDING; RECOGNITION; MUTATION;
Keywords:
cannabinoids; CB2 receptor; G protein; site-directed mutagenesis; adenylyl cyclase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Vogel, Z Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 76100 Rehovot, Israel
Citazione:
M.H. Rhee et al., "Functional role of tryptophan residues in the fourth transmembrane domain of the CB2 cannabinoid receptor", J NEUROCHEM, 75(6), 2000, pp. 2485-2491

Abstract

Several tryptophan (Trp) residues are conserved in G protein-coupled receptors (GPCRs). Relatively little is known about the contribution of these residues and especially of those in the fourth transmembrane domain in the function of the CB2 cannabinoid receptor. Replacing W158 (very highly conserved in GPCRs) and W172 (conserved in CB1 and CB2 cannabinoid receptors but not in many other GPCRs) of the human CB2 receptor with A or L or with F or Y produced different results. We found that the conservative change of W172to F or Y retained cannabinoid binding and downstream signaling (inhibition of adenylyl cyclase), whereas removal of the aromatic side chain by mutating W172 to A or L eliminated agonist binding, W158 was even more sensitiveto being mutated. We found that the conservative W158F mutation retained wild-type binding and signaling activities. However, W158Y and W158A mutantscompletely lost ligand binding capacity. Thus, the Trp side chains at positions 158 and 172 seem to have a critical, but different, role in cannabinoid binding to the human CB2 receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 19:09:45