3rif | pdb_00003rif

C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and glutamate.

spinqualitylabelsall models 3rif, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rif is a 15 chain structure with sequence from Caenorhabditis elegans and Mus musculus. The November 2015 RCSB PDB Molecule of the Month feature on Glutamate-gated Chloride Receptors by David Goodsell is 10.2210/rcsb_pdb/mom_2015_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.345Å Ligands: CL, GLU, IVM, LMT, NAG, OCT, UND Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Fast inhibitory neurotransmission is essential for nervous system function and is mediated by binding of inhibitory neurotransmitters to receptors of the Cys-loop family embedded in the membranes of neurons. Neurotransmitter binding triggers a conformational change in the receptor, opening an intrinsic chloride channel and thereby dampening neuronal excitability. Here we present the first three-dimensional structure, to our knowledge, of an inhibitory anion-selective Cys-loop receptor, the homopentameric Caenorhabditis elegans glutamate-gated chloride channel alpha (GluCl), at 3.3 A resolution. The X-ray structure of the GluCl-Fab complex was determined with the allosteric agonist ivermectin and in additional structures with the endogenous neurotransmitter l-glutamate and the open-channel blocker picrotoxin. Ivermectin, used to treat river blindness, binds in the transmembrane domain of the receptor and stabilizes an open-pore conformation. Glutamate binds in the classical agonist site at subunit interfaces, and picrotoxin directly occludes the pore near its cytosolic base. GluCl provides a framework for understanding mechanisms of fast inhibitory neurotransmission and allosteric modulation of Cys-loop receptors. Principles of activation and permeation in an anion-selective Cys-loop receptor.,Hibbs RE, Gouaux E Nature. 2011 May 15. PMID:21572436 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures Monoclonal Antibodies 3D structures

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