3trp: Difference between revisions
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[[ | ==Crystal structure of recombinant rabbit skeletal calsequestrin== | ||
<StructureSection load='3trp' size='340' side='right' caption='[[3trp]], [[Resolution|resolution]] 1.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3trp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TRP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3trq|3trq]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CASQ1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3trp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3trp RCSB], [http://www.ebi.ac.uk/pdbsum/3trp PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CASQ1_RABIT CASQ1_RABIT]] Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle isoform (CASQ1) binds around 80 Ca(2+) ions, while the cardiac isoform (CASQ2) binds approximately 60 Ca(2+) ions (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Calsequestrin, the major calcium-storage protein of both cardiac and skeletal muscle, binds large amounts of Ca2+ in the sarcoplasmic reticulum and releases them during muscle contraction. For the first time, crystal structures of Ca2+-complexes for both human (hCASQ1) and rabbit skeletal calsequestrin (rCASQ1) were determined, clearly defining its Ca2+-sequestration capabilities through resolution of high- and low-affinity Ca2+-binding sites. rCASQ1 crystallized in low CaCl2 buffer revealed three high-affinity Ca2+ sites with trigonal bipyramidal, octahedral, and pentagonal bipyramidal coordination geometries, along with three low-affinity Ca2+ sites. hCASQ1 crystallized in high CaCl2 showed fifteen Ca2+ ions, which included the six Ca2+ ions in rCASQ1. Most of the low-affinity sites, some of which were mu-carboxylate-bridged, were established by the rotation of dimeric interfaces, indicating cooperative Ca2+-binding that is consistent with our atomic absorption spectroscopic data. Based on these findings, we propose a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca2+-binding activity of calsequestrin. | |||
High-capacity Ca2+-binding of human skeletal calsequestrin.,Sanchez EJ, Lewis KM, Danna BR, Kang C J Biol Chem. 2012 Feb 15. PMID:22337878<ref>PMID:22337878</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Kang, C | [[Category: Kang, C]] | ||
[[Category: Lewis, K M | [[Category: Lewis, K M]] | ||
[[Category: Munske, G R | [[Category: Munske, G R]] | ||
[[Category: Nissen, M S | [[Category: Nissen, M S]] | ||
[[Category: Sanchez, E J | [[Category: Sanchez, E J]] | ||
[[Category: Calcium-binding protein]] | [[Category: Calcium-binding protein]] | ||