1ho2: Difference between revisions

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-[[Image:1ho2.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1ho2", creates the "Structure Box" on the page.
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-{{STRUCTURE_1ho2|  PDB=1ho2  |  SCENE=  }}
-'''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]]' 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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-HO2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO2 OCA].
+</div>
+<div class="pdbe-citations 1ho2" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/12023222 12023222]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Drosophila melanogaster]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Gorlach, M.]]
+[[Category: Gorlach M]]
-[[Category: Haris, P I.]]
+[[Category: Haris PI]]
-[[Category: Hojo, H.]]
+[[Category: Hojo H]]
-[[Category: Ohlenschlager, O.]]
+[[Category: Ohlenschlager O]]
-[[Category: Ramachandran, R.]]
+[[Category: Ramachandran R]]
-[[Category: Alpha-helix]]
-[[Category: Amphipathic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:03:33 2008''