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| | <StructureSection load='2i2r' size='340' side='right'caption='[[2i2r]], [[Resolution|resolution]] 3.35Å' scene=''> | | <StructureSection load='2i2r' size='340' side='right'caption='[[2i2r]], [[Resolution|resolution]] 3.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2i2r]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I2R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2i2r]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I2R FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.35Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kcnd3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), KCNIP1, KCHIP1, VABP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2i2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2r OCA], [https://pdbe.org/2i2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i2r RCSB], [https://www.ebi.ac.uk/pdbsum/2i2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i2r ProSAT]</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=2i2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2r OCA], [https://pdbe.org/2i2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i2r RCSB], [https://www.ebi.ac.uk/pdbsum/2i2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i2r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/KCND3_RAT KCND3_RAT]] Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.<ref>PMID:8831489</ref> <ref>PMID:8734615</ref> <ref>PMID:9001401</ref> <ref>PMID:9450548</ref> [[https://www.uniprot.org/uniprot/KCIP1_HUMAN KCIP1_HUMAN]] 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 KCND1/Kv4.1 and KCND2/Kv4.2 currents. Seems to be involved in KCND2 trafficking to the cell surface.<ref>PMID:10676964</ref> <ref>PMID:11423117</ref> <ref>PMID:12829703</ref>
| + | [https://www.uniprot.org/uniprot/KCND3_RAT KCND3_RAT] Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.<ref>PMID:8831489</ref> <ref>PMID:8734615</ref> <ref>PMID:9001401</ref> <ref>PMID:9450548</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Findeisen, F]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Minor, D L]] | + | [[Category: Findeisen F]] |
| - | [[Category: Pioletti, M]] | + | [[Category: Minor Jr DL]] |
| - | [[Category: Calcium binding protein]] | + | [[Category: Pioletti M]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Ef-hand protein]]
| + | |
| - | [[Category: Ncs protein]]
| + | |
| - | [[Category: Potassium channel]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
KCND3_RAT Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function.
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer.,Pioletti M, Findeisen F, Hura GL, Minor DL Jr Nat Struct Mol Biol. 2006 Nov;13(11):987-95. Epub 2006 Oct 22. PMID:17057713[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dixon JE, Shi W, Wang HS, McDonald C, Yu H, Wymore RS, Cohen IS, McKinnon D. Role of the Kv4.3 K+ channel in ventricular muscle. A molecular correlate for the transient outward current. Circ Res. 1996 Oct;79(4):659-68. PMID:8831489
- ↑ Serodio P, Vega-Saenz de Miera E, Rudy B. Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain. J Neurophysiol. 1996 May;75(5):2174-9. PMID:8734615
- ↑ Tsaur ML, Chou CC, Shih YH, Wang HL. Cloning, expression and CNS distribution of Kv4.3, an A-type K+ channel alpha subunit. FEBS Lett. 1997 Jan 3;400(2):215-20. PMID:9001401
- ↑ Ohya S, Tanaka M, Oku T, Asai Y, Watanabe M, Giles WR, Imaizumi Y. Molecular cloning and tissue distribution of an alternatively spliced variant of an A-type K+ channel alpha-subunit, Kv4.3 in the rat. FEBS Lett. 1997 Dec 22;420(1):47-53. PMID:9450548
- ↑ Pioletti M, Findeisen F, Hura GL, Minor DL Jr. Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer. Nat Struct Mol Biol. 2006 Nov;13(11):987-95. Epub 2006 Oct 22. PMID:17057713 doi:10.1038/nsmb1164
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