1s6c

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[[Image:1s6c.jpg|left|200px]]
 
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==Crystal structure of the complex between KChIP1 and Kv4.2 N1-30==
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The line below this paragraph, containing "STRUCTURE_1s6c", creates the "Structure Box" on the page.
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<StructureSection load='1s6c' size='340' side='right'caption='[[1s6c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1s6c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6C FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#8491;</td></tr>
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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=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
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{{STRUCTURE_1s6c| PDB=1s6c | SCENE= }}
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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=1s6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6c OCA], [https://pdbe.org/1s6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6c RCSB], [https://www.ebi.ac.uk/pdbsum/1s6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KCIP1_RAT KCIP1_RAT] 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 (By similarity).<ref>PMID:12646414</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/s6/1s6c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1s6c 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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Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs.
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'''Crystal structure of the complex between KChIP1 and Kv4.2 N1-30'''
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Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels.,Zhou W, Qian Y, Kunjilwar K, Pfaffinger PJ, Choe S Neuron. 2004 Feb 19;41(4):573-86. PMID:14980206<ref>PMID:14980206</ref>
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==Overview==
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Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1S6C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6C OCA].
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</div>
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<div class="pdbe-citations 1s6c" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels., Zhou W, Qian Y, Kunjilwar K, Pfaffinger PJ, Choe S, Neuron. 2004 Feb 19;41(4):573-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14980206 14980206]
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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[[Category: Protein complex]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Choe, S.]]
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[[Category: Choe S]]
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[[Category: Kunjilwar, K.]]
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[[Category: Kunjilwar K]]
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[[Category: Pfaffinger, P J.]]
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[[Category: Pfaffinger PJ]]
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[[Category: Qian, Y.]]
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[[Category: Qian Y]]
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[[Category: Zhou, W.]]
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[[Category: Zhou W]]
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[[Category: Ef-hand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:21:27 2008''
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Current revision

Crystal structure of the complex between KChIP1 and Kv4.2 N1-30

PDB ID 1s6c

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