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A selective metabotropic glutamate receptor 7 agonist: activation of receptor signaling via an allosteric site modulates stress parameters in vivo.
TLDR
An mGluR7-selective agonist, N,N'-dibenzhydrylethane-1,2-diamine dihydrochloride (AMN082), which directly activates receptor signaling via an allosteric site in the transmembrane domain is characterized and provided evidence for full agonist activity mediated by the heptahelical domain of family 3 G protein-coupled receptors that may lead to drug development opportunities.
CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding.
TLDR
It is proposed that the interaction of CPCCOEt with Thr815 and Ala818 of mGluR1 disrupts receptor activation by inhibiting an intramolecular interaction between the agonist-bound extracellular domain and the transmembrane domain.
The Non-competitive Antagonists 2-Methyl-6-(phenylethynyl)pyridine and 7-Hydroxyiminocyclopropan[b]chromen-1a-carboxylic Acid Ethyl Ester Interact with Overlapping Binding Pockets in the
TLDR
Results indicate that MPEP and CPCCOEt bind to overlapping binding pockets in the TM region of group I mGluRs but interact with different non-conserved residues.
Potential anxiolytic‐ and antidepressant‐like effects of MPEP, a potent, selective and systemically active mGlu5 receptor antagonist
TLDR
The data suggest that selective mGlu5 receptor antagonists may play a role in the therapy of anxiety and/or depression, further studies are required to identify the sites and the mechanism of action of MPEP.
Anxiolytic-like effects of the prototypical metabotropic glutamate receptor 5 antagonist 2-methyl-6-(phenylethynyl)pyridine in rodents.
TLDR
Findings indicate that MPEP exhibits anxiolytic-like effects and low risks for sedation and psychotomimetic side-effects in rodents.
Mutagenesis and Modeling of the GABAB Receptor Extracellular Domain Support a Venus Flytrap Mechanism for Ligand Binding*
TLDR
A three-dimensional model of the LBP-like domain of the GABAB receptor was constructed based on the known structure of LBP and proposes that the initial step in the activation of the receptor by agonist results from the closure of the two lobes of the binding domain.
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