3auw

Cytoplasmic domain of inward rectifier potassium channel Kir3.2 in complex with cadmium

spinqualitylabelsall models 3auw, resolution 3.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3auw is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD, EOH, MG Related: 3agw, 2e4f Gene: Kcnj6 (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The gate at the pore-forming domain of potassium channels is allosterically controlled by a stimulus-sensing domain. Using Cd(2)(+) as a probe, we examined the structural elements responsible for gating in an inward-rectifier K(+) channel (Kir3.2). One of four endogenous cysteines facing the cytoplasm contributes to a high-affinity site for inhibition by internal Cd(2)(+). Crystal structure of its cytoplasmic domain in complex with Cd(2)(+) reveals that octahedral coordination geometry supports the high-affinity binding. This mode of action causes the tethering of the N-terminus to CD loop in the stimulus-sensing domain, suggesting that their conformational changes participate in gating and Cd(2)(+) inhibits Kir3.2 by trapping the conformation in the closed state like "inverse agonist". Inverse agonist-like action of cadmium on G-protein-gated inward-rectifier K(+) channels.,Inanobe A, Matsuura T, Nakagawa A, Kurachi Y Biochem Biophys Res Commun. 2011 Apr 8;407(2):366-71. Epub 2011 Mar 17. PMID:21396912 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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