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New page: left|200px<br /><applet load="2qvk" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qvk, resolution 1.451Å" /> '''The second Ca2+-bin...
 
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[[Image:2qvk.jpg|left|200px]]<br /><applet load="2qvk" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2qvk, resolution 1.451&Aring;" />
'''The second Ca2+-binding domain of the Na+-Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis'''<br />


==Overview==
==The second Ca2+-binding domain of the Na+-Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis==
The Na(+)-Ca(2+) exchanger plays a central role in cardiac contractility, by maintaining Ca(2+) homeostasis. Two Ca(2+)-binding domains,CBD1 and, CBD2, located in a large intracellular loop, regulate activity of the, exchanger. Ca(2+) binding to these regulatory domains activates the, transport of Ca(2+) across the plasma membrane.Previously, we solved the, structure of CBD1, revealing four Ca(2+)ions arranged in a tight planar, cluster. Here, we present structures of CBD2 in the Ca(2+)-bound (1.7-A, resolution) and -free (1.4-Aresolution) conformations Like CBD1, CBD2 has, a classical Ig fold but coordinates only two Ca(2+) ions in primary and, secondary Ca(2+) sites. In the absence of Ca(2+), Lys(585) stabilizes the, structure by coordinating two acidic residues (Asp(552) and Glu(648)), one, from each of the Ca(2+)-binding sites, and prevents a substantial protein, unfolding. We have mutated all of the acidic residues that coordinate the, Ca(2+) ions and have examined the effects of these mutations on regulation, of exchange activity. Three mutations (E516L, D578V, and E648L) at the, primary Ca(2+) site completely remove Ca(2+) regulation, placing the, exchanger into a constitutively active state. These are the first data, defining the role of CBD2 as a regulatory domain in the Na(+)-Ca(2+), exchanger.
<StructureSection load='2qvk' size='340' side='right'caption='[[2qvk]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2qvk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QVK FirstGlance]. <br>
2QVK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QVK OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.451&#8491;</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=2qvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qvk OCA], [https://pdbe.org/2qvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qvk RCSB], [https://www.ebi.ac.uk/pdbsum/2qvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qvk ProSAT]</span></td></tr>
==Reference==
</table>
The second Ca2+-binding domain of the Na+ Ca2+exchanger is essential for regulation: Crystal structures and mutational analysis., Mercado Besserer G, Ottolia M, Nicoll DA, Chaptal V, Cascio D, Philipson KD, Abramson J, Proc Natl Acad Sci U S A. 2007 Oct 25;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17962412 17962412]
== Function ==
[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>
== 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/qv/2qvk_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=2qvk ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abramson, J.]]
[[Category: Abramson J]]
[[Category: Besserer, G.Mercado.]]
[[Category: Cascio D]]
[[Category: Cascio, D.]]
[[Category: Chaptal V]]
[[Category: Chaptal, V.]]
[[Category: Mercado Besserer G]]
[[Category: calcium binding domain]]
[[Category: cbd2]]
[[Category: metal binding protein]]
[[Category: sodium calcium exchanger]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:03:38 2008''

Latest revision as of 09:18, 21 February 2024

The second Ca2+-binding domain of the Na+-Ca2+ exchanger is essential for regulation: crystal structures and mutational analysis

2qvk, resolution 1.45Å

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