8dn5

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Current revision (11:53, 30 October 2024) (edit) (undo)
 
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== Disease ==
== Disease ==
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[https://www.uniprot.org/uniprot/GLRB_HUMAN GLRB_HUMAN] Hereditary hyperekplexia. The disease is caused by variants affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/GLRA1_HUMAN GLRA1_HUMAN] Defects in GLRA1 are the cause of hyperekplexia, hereditary, type 1 (HKPX1) [MIM:[https://omim.org/entry/149400 149400]. A neurologic disorder characterized by muscular rigidity of central nervous system origin, particularly in the neonatal period, and by an exaggerated startle response to unexpected acoustic or tactile stimuli.<ref>PMID:8298642</ref> [:]<ref>PMID:7925268</ref> <ref>PMID:7981700</ref> <ref>PMID:7881416</ref> <ref>PMID:7611730</ref> <ref>PMID:8571969</ref> <ref>PMID:8733061</ref> <ref>PMID:9067762</ref> <ref>PMID:10514101</ref> <ref>PMID:9920650</ref>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/GLRB_HUMAN GLRB_HUMAN] Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:8717357, PubMed:15302677, PubMed:16144831, PubMed:22715885, PubMed:25445488, PubMed:11929858, PubMed:23238346). Heteropentameric channels composed of GLRB and GLRA1 are activated by lower glycine levels than homopentameric GLRA1 (PubMed:8717357). Plays an important role in the down-regulation of neuronal excitability (PubMed:11929858, PubMed:23238346). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488).<ref>PMID:11929858</ref> <ref>PMID:15302677</ref> <ref>PMID:16144831</ref> <ref>PMID:22715885</ref> <ref>PMID:23238346</ref> <ref>PMID:25445488</ref> <ref>PMID:8717357</ref> [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
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[https://www.uniprot.org/uniprot/GLRA1_HUMAN GLRA1_HUMAN] The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing).
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== Publication Abstract from PubMed ==
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Hetero-pentameric Cys-loop receptors constitute a major type of neurotransmitter receptors that enable signal transmission and processing in the nervous system. Despite intense investigations into their working mechanism and pharmaceutical potentials, how neurotransmitters activate these receptors remains unclear due to the lack of high-resolution structural information in the activated open state. Here we report near-atomic resolution structures resolved in digitonin consistent with all principle functional states of the human alpha1beta GlyR, which is a major Cys-loop receptor that mediates inhibitory neurotransmission in the central nervous system of adults. Glycine binding induces cooperative and symmetric structural rearrangements in the neurotransmitter-binding extracellular domain but asymmetrical pore dilation in the transmembrane domain. Symmetric response in the extracellular domain is consistent with electrophysiological data showing cooperative glycine activation and contribution from both alpha1 and beta subunits. A set of functionally essential but differentially charged amino acid residues in the transmembrane domain of the alpha1 and beta subunits explains asymmetric activation. These findings provide a foundation for understanding how the gating of the Cys-loop receptor family members diverges to accommodate specific physiological environments.
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Asymmetric gating of a human hetero-pentameric glycine receptor.,Liu X, Wang W Nat Commun. 2023 Oct 11;14(1):6377. doi: 10.1038/s41467-023-42051-6. PMID:37821459<ref>PMID:37821459</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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<references/>

Current revision

Cryo-EM structure of human Glycine Receptor alpha1-beta heteromer, glycine-bound state1(open state)

PDB ID 8dn5

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