Closed state of both binding domains of homodimeric mGlu receptors is required for full activity

Abstract

Membrane receptors, key components in signal transduction, often function as dimers. These include some G protein–coupled receptors such as metabotropic glutamate (mGlu) receptors that have large extracellular domains (ECDs) where agonists bind. How agonist binding in dimeric ECDs activates the effector domains remains largely unknown. The structure of the… (More)
DOI: 10.1038/nsmb794

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Cite this paper

@article{Kniazeff2004ClosedSO, title={Closed state of both binding domains of homodimeric mGlu receptors is required for full activity}, author={Julie Kniazeff and A S Bessis and Damien Maurel and Herv{\'e} Ansanay and Laurent Pr{\'e}zeau and Jean-Philippe Pin}, journal={Nature Structural &Molecular Biology}, year={2004}, volume={11}, pages={706-713} }