1ho7: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1ho7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ho7" /> '''NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGM...
 
OCA (talk | contribs)
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ho7.jpg|left|200px]]<br /><applet load="1ho7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ho7" />
'''NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE'''<br />


==Overview==
==NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE==
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.
<StructureSection load='1ho7' size='340' side='right'caption='[[1ho7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ho7]] 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=1HO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HO7 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=1ho7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ho7 OCA], [https://pdbe.org/1ho7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ho7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ho7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ho7 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.


==About this Structure==
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>
1HO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HO7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12023222 12023222]
</div>
<div class="pdbe-citations 1ho7" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[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: helix]]
[[Category: peptide]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:42:24 2007''

Latest revision as of 18:38, 29 November 2023

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA