2nz0: Difference between revisions

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-[[Image:2nz0.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2nz0", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2nz0|  PDB=2nz0  |  SCENE=  }}
-'''Crystal structure of potassium channel Kv4.3 in complex with its regulatory subunit KChIP1 (CASP Target)'''
+==Crystal structure of potassium channel Kv4.3 in complex with its regulatory subunit KChIP1 (CASP Target)==
+<StructureSection load='2nz0' size='340' side='right'caption='[[2nz0]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2nz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NZ0 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=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=2nz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nz0 OCA], [https://pdbe.org/2nz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nz0 RCSB], [https://www.ebi.ac.uk/pdbsum/2nz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nz0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/2nz0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2nz0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+KChIPs coassemble with pore-forming Kv4 alpha subunits to form a native complex in the brain and heart and regulate the expression and gating properties of Kv4 K(+) channels, but the mechanisms underlying these processes are unknown. Here we report a co-crystal structure of the complex of human Kv4.3 N-terminus and KChIP1 at a 3.2-A resolution. The structure reveals a unique clamping action of the complex, in which a single KChIP1 molecule, as a monomer, laterally clamps two neighboring Kv4.3 N-termini in a 4:4 manner, forming an octamer. The proximal N-terminal peptide of Kv4.3 is sequestered by its binding to an elongated groove on the surface of KChIP1, which is indispensable for the modulation of Kv4.3 by KChIP1, and the same KChIP1 molecule binds to an adjacent T1 domain to stabilize the tetrameric Kv4.3 channels. Taken together with biochemical and functional data, our findings provide a structural basis for the modulation of Kv4 by KChIPs.
-==Overview==
+Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits.,Wang H, Yan Y, Liu Q, Huang Y, Shen Y, Chen L, Chen Y, Yang Q, Hao Q, Wang K, Chai J Nat Neurosci. 2007 Jan;10(1):32-9. Epub 2006 Dec 24. PMID:17187064<ref>PMID:17187064</ref>
-KChIPs coassemble with pore-forming Kv4 alpha subunits to form a native complex in the brain and heart and regulate the expression and gating properties of Kv4 K(+) channels, but the mechanisms underlying these processes are unknown. Here we report a co-crystal structure of the complex of human Kv4.3 N-terminus and KChIP1 at a 3.2-A resolution. The structure reveals a unique clamping action of the complex, in which a single KChIP1 molecule, as a monomer, laterally clamps two neighboring Kv4.3 N-termini in a 4:4 manner, forming an octamer. The proximal N-terminal peptide of Kv4.3 is sequestered by its binding to an elongated groove on the surface of KChIP1, which is indispensable for the modulation of Kv4.3 by KChIP1, and the same KChIP1 molecule binds to an adjacent T1 domain to stabilize the tetrameric Kv4.3 channels. Taken together with biochemical and functional data, our findings provide a structural basis for the modulation of Kv4 by KChIPs.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-NZ0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZ0 OCA].
+</div>
+<div class="pdbe-citations 2nz0" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits., Wang H, Yan Y, Liu Q, Huang Y, Shen Y, Chen L, Chen Y, Yang Q, Hao Q, Wang K, Chai J, Nat Neurosci. 2007 Jan;10(1):32-9. Epub 2006 Dec 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17187064 17187064]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Chen, L.]]
+[[Category: Chen L]]
-[[Category: Shen, Y.]]
+[[Category: Shen Y]]
-[[Category: Wang, H.]]
+[[Category: Wang H]]
-[[Category: Wang, K.]]
+[[Category: Wang K]]
-[[Category: Yan, Y.]]
+[[Category: Yan Y]]
-[[Category: Kchip1]]
-[[Category: Kv4 3]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:05:56 2008''