1ho7

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE

spinqualitylabelsall models 1ho7, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ho7 is a 1 chain structure with sequence from Drosophila melanogaster. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ho2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KCNAS_DROME] Voltage-dependent potassium channel involved in regulation of sleep need or efficiency. Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Publication Abstract from PubMed The propagation of action potentials during neuronal signal transduction in phospholipid membranes is mediated by ion channels, a diverse group of membrane proteins. The S4-S5 linker peptide (S4-S5), that connects the S4 and S5 transmembrane segments of voltage-gated potassium channels is an important region of the Shaker ion-channel protein. Despite its importance, very little is known about its structure. Here we provide evidence for an amphipathic alpha-helical conformation of a synthetic S4-S5 peptide of the voltage-gated Drosophila melanogaster Shaker potassium channel in water/trifluoroethanol and in aqueous phospholipid micelles. The three-dimensional solution structures of the S4-S5 peptide were obtained by high-resolution nuclear magnetic resonance spectroscopy and distance-geometry/simulated-annealing calculations. The detailed structural features are discussed with respect to model studies and available mutagenesis data on the mechanism and selectivity of the potassium channel. Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel.,Ohlenschlager O, Hojo H, Ramachandran R, Gorlach M, Haris PI Biophys J. 2002 Jun;82(6):2995-3002. PMID:12023222 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Potassium Channel

Proteopedia Page Contributors and Editors (what is this?)

OCA