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Structure paper

TitleStructures of metabotropic GABA receptor.
Journal, issue, pagesNature, Year 2020
Publish dateJun 24, 2020
AuthorsMakaía M Papasergi-Scott / Michael J Robertson / Alpay B Seven / Ouliana Panova / Jesper M Mathiesen / Georgios Skiniotis /
PubMed AbstractGABA (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 linksPubMed:32580208 / Publisher's page
KeywordsSIGNALING PROTEIN / Inhibitor / Heterodimer / GPCR / Homodimer
MethodsEM (single particle)
Resolution3.2 - 3.6 A
Structure data

PDB-6w2x:
CryoEM Structure of Inactive GABAB Heterodimer

PDB-6w2y:
CryoEM Structure of GABAB1b Homodimer

EMDB-21533:
CryoEM Structure of Inactive GABAB Heterodimer

EMDB-21534:
CryoEM Structure of GABAB1b Homodimer

Chemicals

ChemComp-NAG:
Unknown entry

ChemComp-L9Q:
Unknown entry

ChemComp-SGG:
Unknown entry

ChemComp-MG:
MAGNESIUM ION / Magnesium

Source
  • Homo sapiens (human)

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