6jv2: Difference between revisions
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The | ==Structure of RyR2 (P/L-Ca2+/Ca2+-CaM dataset)== | ||
<StructureSection load='6jv2' size='340' side='right'caption='[[6jv2]], [[Resolution|resolution]] 4.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jv2]] is a 8 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=6JV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JV2 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=ZN:ZINC+ION'>ZN</scene></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=6jv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jv2 OCA], [http://pdbe.org/6jv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jv2 RCSB], [http://www.ebi.ac.uk/pdbsum/6jv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jv2 ProSAT]</span></td></tr> | |||
</table> | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6jv2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | |||
[[Category: Chi, X M]] | |||
[[Category: Gong, D S]] | |||
[[Category: Huang, G X.Y]] | |||
[[Category: Lei, J L]] | |||
[[Category: Yan, N]] | |||
[[Category: Zhou, G W]] | |||
[[Category: Cryo-em]] | |||
[[Category: Membrane protein]] | |||
Revision as of 10:43, 17 July 2019
Structure of RyR2 (P/L-Ca2+/Ca2+-CaM dataset)
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