1ho2

From Proteopedia

(Difference between revisions)

Current revision

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES

Structural highlights

1ho2 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.

References

↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ho2"

@@ Line 1: / Line 1: @@
 ==NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES==
-<StructureSection load='1ho2' size='340' side='right'caption='[[1ho2]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<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='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>
+</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>
+[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 ==
@@ Line 26: / Line 27: @@
 [[Category: Drosophila melanogaster]]
 [[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]]
-[[Category: Membrane protein]]

1ho2

From Proteopedia

Current revision

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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