Heptahelical Domain of Metabotropic Glutamate Receptor 5 Behaves Like Rhodopsin-like Receptors

Although agonists bind directly in the heptahelical domain (HD) of most class-I rhodopsin-like G protein coupled receptors (GPCRs), class-III agonists bind in the extracellular domain of their receptors. Indeed, the latter possess a large extracellular domain composed of a cysteine-rich domain and a...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2004-01, Vol.101 (1), p.378-383
Hauptverfasser:	Goudet, Cyril, Gaven, Florence, Kniazeff, Julie, Vol, Claire, Liu, Jiangfeng, Cohen-Gonsaud, Martin, Acher, Francine, Prézeau, Laurent, Pin, Jean Philippe
Format:	Artikel
Sprache:	eng
Schlagworte:	Agonists Allosteric Regulation Animals Biological Sciences Brain Cell Line Cell Membrane Cell Membrane - metabolism Cells Dimers HEK293 cells Humans Hydrazines Hydrazines - pharmacology In Vitro Techniques Kinetics Life Sciences Ligands Metabotropic glutamate receptors Models, Molecular Modulated signal processing Neurons and Cognition Peptide Fragments Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Pharmaceutical sciences Pharmacology Plasmids Protein Structure, Tertiary Proteins Pyridines Pyridines - pharmacology Quisqualic acid Rats Receptor, Metabotropic Glutamate 5 Receptors Receptors, Metabotropic Glutamate Receptors, Metabotropic Glutamate - chemistry Receptors, Metabotropic Glutamate - genetics Receptors, Metabotropic Glutamate - metabolism Recombinant Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Rhodopsin Rhodopsin - metabolism Sequence Deletion
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!