1ho2: Difference between revisions
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==NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES== | ==NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES== | ||
<StructureSection load='1ho2' size='340' side='right'caption='[[1ho2 | <StructureSection load='1ho2' size='340' side='right'caption='[[1ho2]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ho2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ho2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HO2 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ho2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho2 OCA], [https://pdbe.org/1ho2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ho2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ho2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ho2 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KCNAS_DROME 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.<ref>PMID:15858564</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Potassium | *[[Potassium channel 3D structures|Potassium channel 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gorlach | [[Category: Gorlach M]] | ||
[[Category: Haris | [[Category: Haris PI]] | ||
[[Category: Hojo | [[Category: Hojo H]] | ||
[[Category: Ohlenschlager | [[Category: Ohlenschlager O]] | ||
[[Category: Ramachandran | [[Category: Ramachandran R]] | ||
Latest revision as of 21:38, 29 November 2023
NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLESNMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES
Structural highlights
FunctionKCNAS_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.[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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