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1a8y: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8Y FirstGlance]. <br>
</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=1a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8y OCA], [https://pdbe.org/1a8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8y RCSB], [https://www.ebi.ac.uk/pdbsum/1a8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8y ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=1a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8y OCA], [https://pdbe.org/1a8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8y RCSB], [https://www.ebi.ac.uk/pdbsum/1a8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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).  
[https://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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1a8y ConSurf].
</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=1a8y ConSurf].
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== Publication Abstract from PubMed ==
Calsequestrin, the major Ca2+ storage protein of muscle, coordinately binds and releases 40-50 Ca2+ ions per molecule for each contraction-relaxation cycle by an uncertain mechanism. We have determined the structure of rabbit skeletal muscle calsequestrin. Three very negative thioredoxin-like domains surround a hydrophilic center. Each monomer makes two extensive dimerization contacts, both of which involve the approach of many negative groups. This structure suggests a mechanism by which calsequestrin may achieve high capacity Ca2+ binding. The suggested mechanism involves Ca2+-induced collapse of the three domains and polymerization of calsequestrin monomers arising from three factors: N-terminal arm exchange, helix-helix contacts and Ca2+ cross bridges. This proposed structure-based mechanism accounts for the observed coupling of high capacity Ca2+ binding with protein precipitation.
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum.,Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH Nat Struct Biol. 1998 Jun;5(6):476-83. PMID:9628486<ref>PMID:9628486</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1a8y" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Dunker, A K]]
[[Category: Dunker AK]]
[[Category: Kang, C]]
[[Category: Kang C]]
[[Category: Liao, H]]
[[Category: Liao H]]
[[Category: Trumble, W R]]
[[Category: Trumble WR]]
[[Category: Wang, S]]
[[Category: Wang S]]
[[Category: Wesson, C R]]
[[Category: Wesson CR]]
[[Category: Calcium-binding protein]]
[[Category: Calsequestrin]]
[[Category: Rabbit skeletal muscle]]
[[Category: Sarcoplasmic reticulum]]

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