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| | ==Structural Basis of KChIP4a Modulation of Kv4.3 Slow Inactivation== | | ==Structural Basis of KChIP4a Modulation of Kv4.3 Slow Inactivation== |
| - | <StructureSection load='3dd4' size='340' side='right' caption='[[3dd4]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='3dd4' size='340' side='right'caption='[[3dd4]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[3dd4]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dd4 OCA], [https://pdbe.org/3dd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3dd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dd4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KCIP4_MOUSE KCIP4_MOUSE]] Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND3/Kv4.3 and KCND2/Kv4.2 currents (By similarity).<ref>PMID:11805342</ref> <ref>PMID:19109250</ref> | + | [https://www.uniprot.org/uniprot/KCIP4_MOUSE KCIP4_MOUSE] Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND3/Kv4.3 and KCND2/Kv4.2 currents (By similarity).<ref>PMID:11805342</ref> <ref>PMID:19109250</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3dd4" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[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]]
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| - | [[Category: Ion transport]]
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| - | [[Category: Ionic channel]]
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| - | [[Category: Membrane]]
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| - | [[Category: Potassium]]
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| - | [[Category: Potassium channel]]
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| - | [[Category: Potassium transport]]
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| - | [[Category: Transport]]
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| - | [[Category: Transport protein]]
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| - | [[Category: Voltage-gated channel]]
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| Structural highlights
Function
KCIP4_MOUSE Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND3/Kv4.3 and KCND2/Kv4.2 currents (By similarity).[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holmqvist MH, Cao J, Hernandez-Pineda R, Jacobson MD, Carroll KI, Sung MA, Betty M, Ge P, Gilbride KJ, Brown ME, Jurman ME, Lawson D, Silos-Santiago I, Xie Y, Covarrubias M, Rhodes KJ, Distefano PS, An WF. Elimination of fast inactivation in Kv4 A-type potassium channels by an auxiliary subunit domain. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):1035-40. PMID:11805342 doi:http://dx.doi.org/10.1073/pnas.022509299
- ↑ Liang P, Wang H, Chen H, Cui Y, Gu L, Chai J, Wang K. Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation. J Biol Chem. 2009 Feb 20;284(8):4960-7. Epub 2008 Dec 24. PMID:19109250 doi:10.1074/jbc.M807704200
- ↑ Liang P, Wang H, Chen H, Cui Y, Gu L, Chai J, Wang K. Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation. J Biol Chem. 2009 Feb 20;284(8):4960-7. Epub 2008 Dec 24. PMID:19109250 doi:10.1074/jbc.M807704200
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