2e6w

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[[Image:2e6w.png|left|200px]]
 
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{{STRUCTURE_2e6w| PDB=2e6w | SCENE= }}
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==Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin==
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<StructureSection load='2e6w' size='340' side='right'caption='[[2e6w]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2e6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E6W FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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></td></tr>
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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=2e6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e6w OCA], [https://pdbe.org/2e6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e6w RCSB], [https://www.ebi.ac.uk/pdbsum/2e6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e6w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CSEN_HUMAN CSEN_HUMAN] Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception (By similarity).<ref>PMID:9771752</ref> <ref>PMID:10078534</ref> <ref>PMID:10676964</ref> <ref>PMID:11259376</ref> <ref>PMID:11988022</ref> <ref>PMID:12829703</ref> 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 KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and probably KCND3 trafficking to the cell surface.<ref>PMID:9771752</ref> <ref>PMID:10078534</ref> <ref>PMID:10676964</ref> <ref>PMID:11259376</ref> <ref>PMID:11988022</ref> <ref>PMID:12829703</ref> May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of beta-amyloid formation.<ref>PMID:9771752</ref> <ref>PMID:10078534</ref> <ref>PMID:10676964</ref> <ref>PMID:11259376</ref> <ref>PMID:11988022</ref> <ref>PMID:12829703</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/e6/2e6w_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=2e6w 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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Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling.
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===Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin===
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Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin.,Yu L, Sun C, Mendoza R, Wang J, Matayoshi ED, Hebert E, Pereda-Lopez A, Hajduk PJ, Olejniczak ET Protein Sci. 2007 Nov;16(11):2502-9. PMID:17962406<ref>PMID:17962406</ref>
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{{ABSTRACT_PUBMED_17962406}}
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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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==About this Structure==
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<div class="pdbe-citations 2e6w" style="background-color:#fffaf0;"></div>
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[[2e6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E6W OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:017962406</ref><references group="xtra"/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hajduk, P J.]]
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[[Category: Large Structures]]
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[[Category: Hebert, E.]]
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[[Category: Hajduk PJ]]
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[[Category: Mendoza, R.]]
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[[Category: Hebert E]]
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[[Category: Olejniczak, E T.]]
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[[Category: Mendoza R]]
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[[Category: Pereda-Lopez, A.]]
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[[Category: Olejniczak ET]]
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[[Category: Sun, C.]]
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[[Category: Pereda-Lopez A]]
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[[Category: Yu, L.]]
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[[Category: Sun C]]
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[[Category: Calcium-bound form]]
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[[Category: Yu L]]
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[[Category: Metal binding protein]]
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Current revision

Solution structure and calcium binding properties of EF-hands 3 and 4 of calsenilin

PDB ID 2e6w

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