Full Domain Closure of the Ligand-binding Core of the Ionotropic Glutamate Receptor iGluR5 Induced by the High Affinity Agonist Dysiherbaine and the Functional Antagonist 8,9-Dideoxyneodysiherbaine

The prevailing structural model for ligand activation of ionotropic glutamate receptors posits that agonist efficacy arises from the stability and magnitude of induced domain closure in the ligand-binding core structure. Here we describe an exception to the correlation between ligand efficacy and do...

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Autori principali: Frydenvang, Karla, Lash, L. Leanne, Naur, Peter, Postila, Pekka A., Pickering, Darryl S., Smith, Caleb M., Gajhede, Michael, Sasaki, Makoto, Sakai, Ryuichi, Pentikaïnen, Olli T., Swanson, Geoffrey T., Kastrup, Jette S.
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Society for Biochemistry and Molecular Biology 2009
Soggetti:
Mechanisms of Signal Transduction
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2682870/
https://ncbi.nlm.nih.gov/pubmed/19297335
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M808547200
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