8fe1 | pdb_00008fe1

Alpha1/BetaB Heteromeric Glycine Receptor in 1 mM Glycine 20 uM Ivermectin State

spinqualitylabelsall models 8fe1, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8fe1 is a 5 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: D10, GLY, IVM, NAG, PLM, PX4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLRA1_DANRE Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:10188956, PubMed:26344198). Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol (By similarity).[UniProtKB:P23415] Publication Abstract from PubMed Glycine Receptors (GlyRs) provide inhibitory neuronal input in the spinal cord and brainstem, which is critical for muscle coordination and sensory perception. Synaptic GlyRs are a heteromeric assembly of alpha and beta subunits. Here we present cryo-EM structures of full-length zebrafish alpha1beta(B)GlyR in the presence of an antagonist (strychnine), agonist (glycine), or agonist with a positive allosteric modulator (glycine/ivermectin). Each structure shows a distinct pore conformation with varying degrees of asymmetry. Molecular dynamic simulations found the structures were in a closed (strychnine) and desensitized states (glycine and glycine/ivermectin). Ivermectin binds at all five interfaces, but in a distinct binding pose at the beta-alpha interface. Subunit-specific features were sufficient to solve structures without a fiduciary marker and to confirm the 4alpha:1beta stoichiometry recently observed. We also report features of the extracellular and intracellular domains. Together, our results show distinct compositional and conformational properties of alpha(1)betaGlyR and provide a framework for further study of this physiologically important channel. Conformational transitions and allosteric modulation in a heteromeric glycine receptor.,Gibbs E, Klemm E, Seiferth D, Kumar A, Ilca SL, Biggin PC, Chakrapani S Nat Commun. 2023 Mar 13;14(1):1363. doi: 10.1038/s41467-023-37106-7. PMID:36914669 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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