1ho2: Difference between revisions
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==NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES== | |||
<StructureSection load='1ho2' size='340' side='right'caption='[[1ho2]]' scene=''> | |||
== Structural highlights == | |||
<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='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> | |||
== 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;"> | |||
== 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<ref>PMID:12023222</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ho2" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Potassium | *[[Potassium channel 3D structures|Potassium channel 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Gorlach | [[Category: Large Structures]] | ||
[[Category: Haris | [[Category: Gorlach M]] | ||
[[Category: Hojo | [[Category: Haris PI]] | ||
[[Category: Ohlenschlager | [[Category: Hojo H]] | ||
[[Category: Ramachandran | [[Category: Ohlenschlager O]] | ||
[[Category: Ramachandran R]] | |||
