2i2r

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[[Image:2i2r.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the KChIP1/Kv4.3 T1 complex==
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|PDB= 2i2r |SIZE=350|CAPTION= <scene name='initialview01'>2i2r</scene>, resolution 3.35&Aring;
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<StructureSection load='2i2r' size='340' side='right'caption='[[2i2r]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
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|GENE= Kcnd3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), KCNIP1, KCHIP1, VABP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2r OCA], [http://www.ebi.ac.uk/pdbsum/2i2r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i2r RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i2/2i2r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2i2r ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of the KChIP1/Kv4.3 T1 complex'''
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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<ref>PMID:17057713</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2i2r" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2I2R is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17057713 17057713]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Findeisen, F.]]
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[[Category: Findeisen F]]
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[[Category: Jr., D L.Minor.]]
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[[Category: Minor Jr DL]]
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[[Category: Pioletti, M.]]
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[[Category: Pioletti M]]
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[[Category: calcium binding protein]]
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[[Category: complex]]
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[[Category: ef-hand protein]]
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[[Category: ncs protein]]
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[[Category: potassium channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:54 2008''
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Current revision

Crystal structure of the KChIP1/Kv4.3 T1 complex

PDB ID 2i2r

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