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6ji8

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==Structure of RyR2 (F/apoCaM dataset)==
==Structure of RyR2 (F/apoCaM dataset)==
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<StructureSection load='6ji8' size='340' side='right'caption='[[6ji8]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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<SX load='6ji8' size='340' side='right' viewer='molstar' caption='[[6ji8]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ji8]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JI8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JI8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ji8]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JI8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=6ji8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ji8 OCA], [http://pdbe.org/6ji8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ji8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ji8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ji8 ProSAT]</span></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=6ji8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ji8 OCA], [https://pdbe.org/6ji8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ji8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ji8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ji8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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[https://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The high-conductance intracellular calcium (Ca(2+)) channel RyR2 is essential for the coupling of excitation and contraction in cardiac muscle. Among various modulators, calmodulin (CaM) regulates RyR2 in a Ca(2+)-dependent manner. Here we reveal the regulatory mechanism by which porcine RyR2 is modulated by human CaM through the structural determination of RyR2 under eight conditions. Apo-CaM and Ca(2+)-CaM bind to distinct but overlapping sites in an elongated cleft formed by the handle, helical and central domains. The shift in CaM-binding sites on RyR2 is controlled by Ca(2+) binding to CaM, rather than to RyR2. Ca(2+)-CaM induces rotations and intradomain shifts of individual central domains, resulting in pore closure of the PCB95 and Ca(2+)-activated channel. By contrast, the pore of the ATP, caffeine and Ca(2+)-activated channel remains open in the presence of Ca(2+)-CaM, which suggests that Ca(2+)-CaM is one of the many competing modulators of RyR2 gating.
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Modulation of cardiac ryanodine receptor 2 by calmodulin.,Gong D, Chi X, Wei J, Zhou G, Huang G, Zhang L, Wang R, Lei J, Chen SRW, Yan N Nature. 2019 Jul 5. pii: 10.1038/s41586-019-1377-y. doi:, 10.1038/s41586-019-1377-y. PMID:31278385<ref>PMID:31278385</ref>
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[FKBP 3D structures|FKBP 3D structures]]
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</div>
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<div class="pdbe-citations 6ji8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
 
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Chi, X M]]
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[[Category: Chi XM]]
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[[Category: Gong, D S]]
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[[Category: Gong DS]]
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[[Category: Huang, G X.Y]]
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[[Category: Huang GXY]]
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[[Category: Lei, J L]]
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[[Category: Lei JL]]
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[[Category: Yan, N]]
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[[Category: Yan N]]
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[[Category: Zhou, G W]]
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[[Category: Zhou GW]]
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[[Category: Cryo-em]]
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[[Category: Membrane protein]]
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Current revision

Structure of RyR2 (F/apoCaM dataset)

6ji8, resolution 3.60Å

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OCA

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