|Title||Structures of metabotropic GABA receptor.|
|Journal, issue, pages||Nature, Year 2020|
|Publish date||Jun 24, 2020|
|Authors||Makaía M Papasergi-Scott / Michael J Robertson / Alpay B Seven / Ouliana Panova / Jesper M Mathiesen / Georgios Skiniotis /|
|PubMed Abstract||GABA (γ-aminobutyric acid) stimulation of the metabotropic GABA receptor results in prolonged inhibition of neurotransmission that is central to brain physiology. GABA belongs to the Family C of G ...GABA (γ-aminobutyric acid) stimulation of the metabotropic GABA receptor results in prolonged inhibition of neurotransmission that is central to brain physiology. GABA belongs to the Family C of G protein-coupled receptors (GPCRs), which operate as dimers to relay synaptic neurotransmitter signals into a cellular response through the binding and activation of heterotrimeric G proteins. GABA, however, is unique in its function as an obligate heterodimer in which agonist binding and G protein activation take place on distinct subunits. Here we show structures of heterodimeric and homodimeric full-length GABA receptors. Complemented by cellular signaling assays and atomistic simulations, the structures reveal an essential role for the GABA extracellular loop 2 (ECL2) in relaying structural transitions by ordering the linker connecting the extracellular ligand-binding domain to the transmembrane region. Furthermore, the ECL2 of both GABA subunits caps and interacts with the hydrophilic head of a phospholipid occupying the extracellular half of the transmembrane domain, thereby providing a potentially crucial link between ligand binding and the receptor core that engages G protein. These results provide a starting framework to decipher mechanistic modes of signal transduction mediated by GABA dimers and have important implications for rational drug design targeting these receptors.|
|External links||PubMed:32580208 / Publisher's page|
|Keywords||SIGNALING PROTEIN / Inhibitor / Heterodimer / GPCR / Homodimer|
|Methods||EM (single particle)|
|Resolution||3.2 - 3.6 A|
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