6wot
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Cryo-EM structure of recombinant rabbit Ryanodine Receptor type 1 mutant R164C in complex with FKBP12.6== |
| - | <StructureSection load='6wot' size='340' side='right'caption='[[6wot]]' scene=''> | + | <StructureSection load='6wot' size='340' side='right'caption='[[6wot]], [[Resolution|resolution]] 3.54Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6wot]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WOT 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=6wot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wot OCA], [https://pdbe.org/6wot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wot RCSB], [https://www.ebi.ac.uk/pdbsum/6wot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wot ProSAT]</span></td></tr> | + | </td></tr><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> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6wot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wot OCA], [https://pdbe.org/6wot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wot RCSB], [https://www.ebi.ac.uk/pdbsum/6wot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wot ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/RYR1_RABIT RYR1_RABIT]] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).<ref>PMID:10388749</ref> <ref>PMID:22036948</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mutations in ryanodine receptors (RyRs), intracellular Ca(2+) channels, are associated with deadly disorders. Despite abundant functional studies, the molecular mechanism of RyR malfunction remains elusive. We studied two single-point mutations at an equivalent site in the skeletal (RyR1 R164C) and cardiac (RyR2 R176Q) isoforms using ryanodine binding, Ca(2+) imaging, and cryo-electron microscopy (cryo-EM) of the full-length protein. Loss of the positive charge had greater effect on the skeletal isoform, mediated via distortion of a salt bridge network, a molecular latch inducing rotation of a cytoplasmic domain, and partial progression to open-state traits of the large cytoplasmic assembly accompanied by alteration of the Ca(2+) binding site, which concur with the major "hyperactive" feature of the mutated channel. Our cryo-EM studies demonstrated the allosteric effect of a mutation situated ~85 A away from the pore and identified an isoform-specific structural effect. | ||
| + | |||
| + | Structural mechanism of two gain-of-function cardiac and skeletal RyR mutations at an equivalent site by cryo-EM.,Iyer KA, Hu Y, Nayak AR, Kurebayashi N, Murayama T, Samso M Sci Adv. 2020 Jul 29;6(31):eabb2964. doi: 10.1126/sciadv.abb2964. eCollection, 2020 Jul. PMID:32832689<ref>PMID:32832689</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6wot" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[FKBP 3D structures|FKBP 3D structures]] | ||
| + | *[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Oryctolagus cuniculus]] |
| + | [[Category: Hu Y]] | ||
| + | [[Category: Iyer KA]] | ||
| + | [[Category: Kurebayashi N]] | ||
| + | [[Category: Murayama T]] | ||
| + | [[Category: Samso M]] | ||
Revision as of 03:44, 8 September 2022
Cryo-EM structure of recombinant rabbit Ryanodine Receptor type 1 mutant R164C in complex with FKBP12.6
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