3ukm

Crystal structure of the human two pore domain potassium ion channel K2P1 (TWIK-1)Crystal structure of the human two pore domain potassium ion channel K2P1 (TWIK-1)

Structural highlights 3ukm is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KCNK1_HUMAN Weakly inward rectifying potassium channel that contributes to the regulation of the resting membrane potential. Publication Abstract from PubMed Two-pore domain potassium (K(+)) channels (K2P channels) control the negative resting potential of eukaryotic cells and regulate cell excitability by conducting K(+) ions across the plasma membrane. Here, we present the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1 (TWIK-1). Unlike other K(+) channel structures, K2P1 is dimeric. An extracellular cap domain located above the selectivity filter forms an ion pathway in which K(+) ions flow through side portals. Openings within the transmembrane region expose the pore to the lipid bilayer and are filled with electron density attributable to alkyl chains. An interfacial helix appears structurally poised to affect gating. The structure lays a foundation to further investigate how K2P channels are regulated by diverse stimuli. Crystal structure of the human two-pore domain potassium channel K2P1.,Miller AN, Long SB Science. 2012 Jan 27;335(6067):432-6. PMID:22282804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Potassium channel 3D structures

spinqualitylabelsall models 3ukm, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image