View source for 1kn7


==Solution structure of the tandem inactivation domain (residues 1-75) of potassium channel RCK4 (Kv1.4)==
<StructureSection load='1kn7' size='340' side='right'caption='[[1kn7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kn7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KN7 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=1kn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn7 OCA], [https://pdbe.org/1kn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kn7 RCSB], [https://www.ebi.ac.uk/pdbsum/1kn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kn7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KCNA4_RAT KCNA4_RAT] 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cumulative inactivation of voltage-gated (Kv) K(+) channels shapes the presynaptic action potential and determines timing and strength of synaptic transmission. Kv1.4 channels exhibit rapid "ball-and-chain"-type inactivation gating. Different from all other Kvalpha subunits, Kv1.4 harbors two inactivation domains at its N terminus. Here we report the solution structure and function of this "tandem inactivation domain" using NMR spectroscopy and patch clamp recordings. Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N terminus anchored at a 5-turn helix, whereas ID2 (residues 40-50) is a 2.5-turn helix made up of small hydrophobic amino acids. Functional analysis suggests that only ID1 may work as a pore-occluding ball domain, whereas ID2 most likely acts as a "docking domain" that attaches ID1 to the cytoplasmic face of the channel. Deletion of ID2 slows inactivation considerably and largely impairs cumulative inactivation. Together, the concerted action of ID1 and ID2 may promote rapid inactivation of Kv1.4 that is crucial for the channel function in short term plasticity.

Solution structure and function of the "tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4.,Wissmann R, Bildl W, Oliver D, Beyermann M, Kalbitzer HR, Bentrop D, Fakler B J Biol Chem. 2003 May 2;278(18):16142-50. Epub 2003 Feb 16. PMID:12590144<ref>PMID:12590144</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1kn7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Bentrop D]]
[[Category: Beyermann M]]
[[Category: Bildl W]]
[[Category: Fakler B]]
[[Category: Kalbitzer HR]]
[[Category: Oliver D]]
[[Category: Wissmann R]]