Serotonin 2A receptor disulfide bridge integrity is crucial for ligand binding to different signalling states but not for its homodimerization-Reference-Cited by-同舟云学术

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Serotonin 2A receptor disulfide bridge integrity is crucial for ligand binding to different signalling states but not for its homodimerization

Published:2017-11 Issue: Volume:815 Page:138-146
ISSN:0014-2999
Container-title:European Journal of Pharmacology
language:en
Short-container-title:European Journal of Pharmacology

Author:

Iglesias Alba,Cimadevila Marta,la Fuente Rocío Ailim de,Martí-Solano María,Cadavid María Isabel,Castro Marián,Selent Jana,Loza María Isabel,Brea José

Funder

Ministerio de Ciencia e Innovacion

Ministerio de Economia y Competitividad

Xunta de Galicia

European Union

Publisher

Elsevier BV

Subject

Pharmacology

Reference65 articles.

1. Probing the existence of G protein-coupled receptor dimers by positive and negative ligand-dependent cooperative binding;Albizu;Mol. Pharmacol.,2006

2. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function;Angers;Annu. Rev. Pharmacol. Toxicol.,2002

3. Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands;Avlani;J. Biol. Chem.,2007

4. Molecular characterization of a purified 5-HT4 receptor: a structural basis for drug efficacy;Banères;J. Biol. Chem.,2005

5. Role of conserved disulfide bridges and aromatic residues in extracellular loop 2 of chemokine receptor CCR8 for chemokine and small molecule binding;Barington;J. Biol. Chem.,2016

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