2xq6 | pdb_00002xq6

PENTAMERIC LIGAND GATED ION CHANNEL GLIC IN COMPLEX WITH CESIUM ION (CS+)

spinqualitylabelsall models 2xq6, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xq6 is a 5 chain structure with sequence from Gloeobacter violaceus pcc 7421. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CS Related: 2xqa, 2xq9, 2xq7, 2xq5, 2xq3, 2xq8, 2xq4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q7NDN8_GLOVI] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change. Publication Abstract from PubMed The flow of ions through cation-selective members of the pentameric ligand-gated ion channel family is inhibited by a structurally diverse class of molecules that bind to the transmembrane pore in the open state of the protein. To obtain insight into the mechanism of channel block, we have investigated the binding of positively charged inhibitors to the open channel of the bacterial homolog GLIC by using X-ray crystallography and electrophysiology. Our studies reveal the location of two regions for interactions, with larger blockers binding in the center of the membrane and divalent transition metal ions binding to the narrow intracellular pore entry. The results provide a structural foundation for understanding the interactions of the channel with inhibitors that is relevant for the entire family. Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel.,Hilf RJ, Bertozzi C, Zimmermann I, Reiter A, Trauner D, Dutzler R Nat Struct Mol Biol. 2010 Nov;17(11):1330-1336. Epub 2010 Oct 31. PMID:21037567 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels

Proteopedia Page Contributors and Editors (what is this?)

OCA