2yn6 | pdb_00002yn6

Pentameric Ligand-Gated Ion Channel ELIC in Complex with Barium

spinqualitylabelsall models 2yn6, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yn6 is a 5 chain structure with sequence from Dickeya dadantii 3937. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.31Å Ligands: BA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E0SJQ4_DICD3 Publication Abstract from PubMed The modulation of pentameric ligand-gated ion channels (pLGICs) by divalent cations is believed to play an important role in their regulation in a physiological context. Ions such as calcium or zinc influence the activity of pLGIC neurotransmitter receptors by binding to their extracellular domain and either potentiate or inhibit channel activation. Here we have investigated by electrophysiology and X-ray crystallography the effect of divalent ions on ELIC, a close prokaryotic pLGIC homologue of known structure. We found that divalent cations inhibit the activation of ELIC by the agonist cysteamine, reducing both its potency and, at higher concentrations, its maximum response. Crystal structures of the channel in complex with barium reveal the presence of several distinct binding sites. By mutagenesis we confirmed that the site responsible for divalent inhibition is located at the outer rim of the extracellular domain, at the interface between adjacent subunits but at some distance from the agonist binding region. Here, divalent cations interact with the protein via carboxylate side-chains, and the site is similar in structure to calcium binding sites described in other proteins. There is evidence that other pLGICs may be regulated by divalent ions binding to a similar region, even though the interacting residues are not conserved within the family. Our study provides structural and functional insight into the allosteric regulation of ELIC and is of potential relevance for the entire family. Inhibition of the Prokaryotic Pentameric Ligand-Gated Ion Channel ELIC by Divalent Cations.,Zimmermann I, Marabelli A, Bertozzi C, Sivilotti LG, Dutzler R PLoS Biol. 2012 Nov;10(11):e1001429. doi: 10.1371/journal.pbio.1001429. Epub 2012, Nov 20. PMID:23185134 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA