5go9: Difference between revisions
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==Cryo-EM structure of RyR2 in closed state== | ==Cryo-EM structure of RyR2 in closed state== | ||
<StructureSection load='5go9' size='340' side='right' caption='[[5go9]], [[Resolution|resolution]] 4.40Å' scene=''> | <StructureSection load='5go9' size='340' side='right'caption='[[5go9]], [[Resolution|resolution]] 4.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5go9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GO9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5go9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GO9 FirstGlance]. <br> | ||
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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=5go9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5go9 OCA], [http://pdbe.org/5go9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5go9 RCSB], [http://www.ebi.ac.uk/pdbsum/5go9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5go9 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=5go9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5go9 OCA], [http://pdbe.org/5go9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5go9 RCSB], [http://www.ebi.ac.uk/pdbsum/5go9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5go9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5go9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5go9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ryanodine receptor|Ryanodine receptor]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Peng, W]] | [[Category: Peng, W]] | ||
Revision as of 10:13, 6 November 2019
Cryo-EM structure of RyR2 in closed stateCryo-EM structure of RyR2 in closed state
Structural highlights
Publication Abstract from PubMedRyR2 is a high-conductance intracellular calcium (Ca2+) channel that controls the release of Ca2+ from the sarco(endo)plasmic reticulum of a variety of cells. Here, we report the structures of RyR2 from porcine heart in both the open and closed states at near-atomic resolutions determined using single-particle electron cryomicroscopy. Structural comparison reveals a breathing motion of the overall cytoplasmic region resulted from the interdomain movements of amino-terminal domains (NTDs), Helical domains, and Handle domains, whereas almost no intradomain shifts are observed in these armadillo repeats-containing domains. Outward rotations of the Central domains, which integrate the conformational changes of the cytoplasmic region, lead to the dilation of the cytoplasmic gate through coupled motions. Our structural and mutational characterizations provide important insights into the gating and disease mechanism of RyRs. Structural basis for the gating mechanism of the type 2 ryanodine receptor RyR2.,Peng W, Shen H, Wu J, Guo W, Pan X, Wang R, Chen SR, Yan N Science. 2016 Oct 21;354(6310). pii: aah5324. Epub 2016 Sep 22. PMID:27708056[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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