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-Structure paper
タイトル | Characterization of the subunit composition and structure of adult human glycine receptors. |
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ジャーナル・号・ページ | Neuron, Vol. 109, Issue 17, Page 2707-22716.e6, Year 2021 |
掲載日 | 2021年9月1日 |
著者 | Hailong Yu / Xiao-Chen Bai / Weiwei Wang / |
PubMed 要旨 | The strychnine-sensitive pentameric glycine receptor (GlyR) mediates fast inhibitory neurotransmission in the mammalian nervous system. Only heteromeric GlyRs mediate synaptic transmission, as they ...The strychnine-sensitive pentameric glycine receptor (GlyR) mediates fast inhibitory neurotransmission in the mammalian nervous system. Only heteromeric GlyRs mediate synaptic transmission, as they contain the β subunit that permits clustering at the synapse through its interaction with scaffolding proteins. Here, we show that α2 and β subunits assemble with an unexpected 4:1 stoichiometry to produce GlyR with native electrophysiological properties. We determined structures in multiple functional states at 3.6-3.8 Å resolutions and show how 4:1 stoichiometry is consistent with the structural features of α2β GlyR. Furthermore, we show that one single β subunit in each GlyR gives rise to the characteristic electrophysiological properties of heteromeric GlyR, while more β subunits render GlyR non-conductive. A single β subunit ensures a univalent GlyR-scaffold linkage, which means the scaffold alone regulates the cluster properties. |
リンク | Neuron / PubMed:34473954 |
手法 | EM (単粒子) |
解像度 | 3.6 - 3.8 Å |
構造データ | EMDB-23041, PDB-7kuy: EMDB-23148, PDB-7l31: |
化合物 | ChemComp-NAG: ChemComp-GLY: ChemComp-SY9: |
由来 |
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キーワード | MEMBRANE PROTEIN / SIGNALING PROTEIN / glycine receptor / alpha2-beta hetero-pentamer / glycine / strychnine |