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==Structure of RyR2 (F/A/C/Ca2+ dataset)==
==Structure of RyR2 (F/A/C/Ca2+ dataset)==
<StructureSection load='6ji0' size='340' side='right'caption='[[6ji0]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<SX load='6ji0' size='340' side='right' viewer='molstar' caption='[[6ji0]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ji0]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=6JI0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JI0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ji0]] is a 8 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=6JI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JI0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFF:CAFFEINE'>CFF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFF:CAFFEINE'>CFF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ji0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ji0 OCA], [https://pdbe.org/6ji0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ji0 RCSB], [https://www.ebi.ac.uk/pdbsum/6ji0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ji0 ProSAT]</span></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=6ji0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ji0 OCA], [http://pdbe.org/6ji0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ji0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ji0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ji0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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>
==See Also==
 
*[[FKBP 3D structures|FKBP 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]]
</div>
<div class="pdbe-citations 6ji0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Chi, X M]]
[[Category: Chi XM]]
[[Category: Gong, D S]]
[[Category: Gong DS]]
[[Category: Huang, G X.Y]]
[[Category: Huang GXY]]
[[Category: Lei, J L]]
[[Category: Lei JL]]
[[Category: Yan, N]]
[[Category: Yan N]]
[[Category: Zhou, G W]]
[[Category: Zhou GW]]
[[Category: Cryo-em]]
[[Category: Membrane protein]]

Latest revision as of 13:38, 27 March 2024

Structure of RyR2 (F/A/C/Ca2+ dataset)Structure of RyR2 (F/A/C/Ca2+ dataset)

6ji0, resolution 4.20Å

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