4h37

Crystal structure of a voltage-gated K+ channel pore domain in a closed state in lipid membranes

spinqualitylabelsall models 4h37, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h37 is a 2 chain structure with sequence from Listeria monocytogenes EGD-e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.35Å Ligands: K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8Y5K1_LISMO Publication Abstract from PubMed Voltage-gated K(+) channels underlie the electrical excitability of cells. Each subunit of the functional tetramer consists of the tandem fusion of two modules, an N-terminal voltage-sensor and a C-terminal pore. To investigate how sensor coupling to the pore generates voltage-dependent channel opening, we solved the crystal structure and characterized the function of a voltage-gated K(+) channel pore in a lipid membrane. The structure of a functional channel in a membrane environment at 3.1 A resolution establishes an unprecedented connection between channel structure and function. The structure is unique in delineating an ion-occupied ready to conduct selectivity filter, a confined aqueous cavity, and a closed activation gate, embodying a dynamic entity trapped in an unstable closed state. Crystal Structure of a Voltage-gated K+ Channel Pore Module in a Closed State in Lipid Membranes.,Santos JS, Asmar-Rovira GA, Han GW, Liu W, Syeda R, Cherezov V, Baker KA, Stevens RC, Montal M J Biol Chem. 2012 Dec 14;287(51):43063-70. doi: 10.1074/jbc.M112.415091. Epub, 2012 Oct 24. PMID:23095758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA