1ho7: Difference between revisions

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[[Image:1ho7.png|left|200px]]


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==NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE==
The line below this paragraph, containing "STRUCTURE_1ho7", creates the "Structure Box" on the page.
<StructureSection load='1ho7' size='340' side='right'caption='[[1ho7]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_1ho7|  PDB=1ho7  |  SCENE=  }}
</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.


===NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ho7" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12023222 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12023222}}
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</StructureSection>
==About this Structure==
1HO7 is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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]
[[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://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:27:46 2008''

Latest revision as of 21:38, 29 November 2023

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFENMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN TFE

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.
Method:Solution NMR
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.[1]

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Cirelli C, Bushey D, Hill S, Huber R, Kreber R, Ganetzky B, Tononi G. Reduced sleep in Drosophila Shaker mutants. Nature. 2005 Apr 28;434(7037):1087-92. PMID:15858564 doi:http://dx.doi.org/nature03486
  2. Ohlenschlager O, Hojo H, Ramachandran R, Gorlach M, Haris PI. Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel. Biophys J. 2002 Jun;82(6):2995-3002. PMID:12023222
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