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2fwu

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{{Seed}}
 
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[[Image:2fwu.png|left|200px]]
 
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==Second Ca2+ binding domain of the Na,Ca-exchanger (NCX1)==
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The line below this paragraph, containing "STRUCTURE_2fwu", creates the "Structure Box" on the page.
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<StructureSection load='2fwu' size='340' side='right'caption='[[2fwu]]' 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'>[[2fwu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FWU 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">Solution NMR</td></tr>
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-->
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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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{{STRUCTURE_2fwu| PDB=2fwu | 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=2fwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fwu OCA], [https://pdbe.org/2fwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fwu RCSB], [https://www.ebi.ac.uk/pdbsum/2fwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fwu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NAC1_CANLF NAC1_CANLF] Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes (PubMed:1700476, PubMed:1785844, PubMed:9486131, PubMed:17962412). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for normal embryonic heart development and the onset of heart contractions (By similarity).[UniProtKB:P70414]<ref>PMID:1700476</ref> <ref>PMID:1785844</ref> <ref>PMID:17962412</ref> <ref>PMID:19332552</ref> <ref>PMID:9486131</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/fw/2fwu_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=2fwu 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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The plasma membrane Na+/Ca2+ exchanger (NCX) is almost certainly the major Ca2+ extrusion mechanism in cardiac myocytes. Binding of Na+ and Ca2+ ions to its large cytosolic loop regulates ion transport of the exchanger. We determined the solution structures of two Ca2+ binding domains (CBD1 and CBD2) that, together with an alpha-catenin-like domain (CLD), form the regulatory exchanger loop. CBD1 and CBD2 are very similar in the Ca2+ bound state and describe the Calx-beta motif. Strikingly, in the absence of Ca2+, the upper half of CBD1 unfolds while CBD2 maintains its structural integrity. Together with a 7-fold higher affinity for Ca2+, this suggests that CBD1 is the primary Ca2+ sensor. Specific point mutations in either domain largely allow the interchange of their functionality and uncover the mechanism underlying Ca2+ sensing in NCX.
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===Second Ca2+ binding domain of the Na,Ca-exchanger (NCX1)===
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Ca2+ regulation in the Na+/Ca2+ exchanger involves two markedly different Ca2+ sensors.,Hilge M, Aelen J, Vuister GW Mol Cell. 2006 Apr 7;22(1):15-25. PMID:16600866<ref>PMID:16600866</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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The line below this paragraph, {{ABSTRACT_PUBMED_16600866}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2fwu" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16600866 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16600866}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2FWU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWU OCA].
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==Reference==
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Ca2+ regulation in the Na+/Ca2+ exchanger involves two markedly different Ca2+ sensors., Hilge M, Aelen J, Vuister GW, Mol Cell. 2006 Apr 7;22(1):15-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16600866 16600866]
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[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aelen, J.]]
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[[Category: Aelen J]]
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[[Category: Hilge, M.]]
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[[Category: Hilge M]]
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[[Category: Vuister, G W.]]
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[[Category: Vuister GW]]
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[[Category: Beta-bulge]]
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[[Category: Beta-sandwich]]
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[[Category: Ca2+ binding]]
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[[Category: Greek key]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:04:29 2008''
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Current revision

Second Ca2+ binding domain of the Na,Ca-exchanger (NCX1)

PDB ID 2fwu

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