3dd4: Difference between revisions
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[[ | ==Structural Basis of KChIP4a Modulation of Kv4.3 Slow Inactivation== | ||
<StructureSection load='3dd4' size='340' side='right' caption='[[3dd4]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3dd4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DD4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kcnip4, Calp, Kchip4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3dd4 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Dynamic inactivation in Kv4 A-type K(+) current plays a critical role in regulating neuronal excitability by shaping action potential waveform and duration. Multifunctional auxiliary KChIP1-4 subunits, which share a high homology in their C-terminal core regions, exhibit distinctive modulation of inactivation and surface expression of pore-forming Kv4 subunits. However, the structural differences that underlie the functional diversity of Kv channel-interacting proteins (KChIPs) remain undetermined. Here we have described the crystal structure of KChIP4a at 3.0A resolution, which shows distinct N-terminal alpha-helices that differentiate it from other KChIPs. Biochemical experiments showed that competitive binding of the Kv4.3 N-terminal peptide to the hydrophobic groove of the core of KChIP4a causes the release of the KChIP4a N terminus that suppresses the inactivation of Kv4.3 channels. Electrophysiology experiments confirmed that the first N-terminal alpha-helix peptide (residues 1-34) of KChIP4a, either by itself or fused to N-terminal truncated Kv4.3, can confer slow inactivation. We propose that N-terminal binding of Kv4.3 to the core of KChIP4a mobilizes the KChIP4a N terminus, which serves as the slow inactivation gate. | |||
Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation.,Liang P, Wang H, Chen H, Cui Y, Gu L, Chai J, Wang K J Biol Chem. 2009 Feb 20;284(8):4960-7. Epub 2008 Dec 24. PMID:19109250<ref>PMID:19109250</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Chai, J | [[Category: Chai, J]] | ||
[[Category: Wang, H | [[Category: Wang, H]] | ||
[[Category: Wang, K | [[Category: Wang, K]] | ||
[[Category: Ef-hands protein]] | [[Category: Ef-hands protein]] | ||
[[Category: Ion transport]] | [[Category: Ion transport]] | ||
Revision as of 11:18, 12 November 2014
Structural Basis of KChIP4a Modulation of Kv4.3 Slow InactivationStructural Basis of KChIP4a Modulation of Kv4.3 Slow Inactivation
Structural highlights
Publication Abstract from PubMedDynamic inactivation in Kv4 A-type K(+) current plays a critical role in regulating neuronal excitability by shaping action potential waveform and duration. Multifunctional auxiliary KChIP1-4 subunits, which share a high homology in their C-terminal core regions, exhibit distinctive modulation of inactivation and surface expression of pore-forming Kv4 subunits. However, the structural differences that underlie the functional diversity of Kv channel-interacting proteins (KChIPs) remain undetermined. Here we have described the crystal structure of KChIP4a at 3.0A resolution, which shows distinct N-terminal alpha-helices that differentiate it from other KChIPs. Biochemical experiments showed that competitive binding of the Kv4.3 N-terminal peptide to the hydrophobic groove of the core of KChIP4a causes the release of the KChIP4a N terminus that suppresses the inactivation of Kv4.3 channels. Electrophysiology experiments confirmed that the first N-terminal alpha-helix peptide (residues 1-34) of KChIP4a, either by itself or fused to N-terminal truncated Kv4.3, can confer slow inactivation. We propose that N-terminal binding of Kv4.3 to the core of KChIP4a mobilizes the KChIP4a N terminus, which serves as the slow inactivation gate. Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation.,Liang P, Wang H, Chen H, Cui Y, Gu L, Chai J, Wang K J Biol Chem. 2009 Feb 20;284(8):4960-7. Epub 2008 Dec 24. PMID:19109250[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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