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Structure paper

TitleStructures of metabotropic GABA receptor.
Journal, issue, pagesNature, Vol. 584, Issue 7820, Page 310-314, Year 2020
Publish dateJun 24, 2020
AuthorsMakaía M Papasergi-Scott / Michael J Robertson / Alpay B Seven / Ouliana Panova / Jesper M Mathiesen / Georgios Skiniotis /
PubMed AbstractStimulation of the metabotropic GABA receptor by γ-aminobutyric acid (GABA) results in prolonged inhibition of neurotransmission, which is central to brain physiology. GABA belongs to family C of ...Stimulation of the metabotropic GABA receptor by γ-aminobutyric acid (GABA) results in prolonged inhibition of neurotransmission, which is central to brain physiology. GABA belongs to family C of the G-protein-coupled receptors, which operate as dimers to transform synaptic neurotransmitter signals into a cellular response through the binding and activation of heterotrimeric G proteins. However, GABA is unique in its function as an obligate heterodimer in which agonist binding and G-protein activation take place on distinct subunits. Here we present cryo-electron microscopy structures of heterodimeric and homodimeric full-length GABA receptors. Complemented by cellular signalling assays and atomistic simulations, these structures reveal that extracellular loop 2 (ECL2) of GABA has an essential role in relaying structural transitions by ordering the linker that connects the extracellular ligand-binding domain to the transmembrane region. Furthermore, the ECL2 of each of the subunits of GABA caps and interacts with the hydrophilic head of a phospholipid that occupies the extracellular half of the transmembrane domain, thereby providing a potentially crucial link between ligand binding and the receptor core that engages G proteins. These results provide a starting framework through which to decipher the mechanistic modes of signal transduction mediated by GABA dimers, and have important implications for rational drug design that targets these receptors.
External linksNature / PubMed:32580208 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.6 Å
Structure data

21533

6w2x

EMDB-21533, PDB-6w2x:
CryoEM Structure of Inactive GABAB Heterodimer
Method: EM (single particle) / Resolution: 3.6 Å

21534

6w2y

EMDB-21534, PDB-6w2y:
CryoEM Structure of GABAB1b Homodimer
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-L9Q:
(1S)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate

ChemComp-SGG:
[(2~{S})-3-[[(1~{S})-1-(3,4-dichlorophenyl)ethyl]amino]-2-oxidanyl-propyl]-(phenylmethyl)phosphinic acid

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Inhibitor / Heterodimer / GPCR / Homodimer

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