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3j8e
From Proteopedia
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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=3j8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j8e RCSB], [http://www.ebi.ac.uk/pdbsum/3j8e PDBsum]</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=3j8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j8e RCSB], [http://www.ebi.ac.uk/pdbsum/3j8e PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ryanodine receptors (RyRs) mediate the rapid release of calcium (Ca2+) from intracellular stores into the cytosol, which is essential for numerous cellular functions including excitation-contraction coupling in muscle. Lack of sufficient structural detail has impeded understanding of RyR gating and regulation. Here we report the closed-state structure of the 2.3-megadalton complex of the rabbit skeletal muscle type 1 RyR (RyR1), solved by single-particle electron cryomicroscopy at an overall resolution of 4.8 A. We fitted a polyalanine-level model to all 3,757 ordered residues in each protomer, defining the transmembrane pore in unprecedented detail and placing all cytosolic domains as tertiary folds. The cytosolic assembly is built on an extended alpha-solenoid scaffold connecting key regulatory domains to the pore. The RyR1 pore architecture places it in the six-transmembrane ion channel superfamily. A unique domain inserted between the second and third transmembrane helices interacts intimately with paired EF-hands originating from the alpha-solenoid scaffold, suggesting a mechanism for channel gating by Ca2+. | ||
| + | |||
| + | Structure of a mammalian ryanodine receptor.,Zalk R, Clarke OB, Georges AD, Grassucci RA, Reiken S, Mancia F, Hendrickson WA, Frank J, Marks AR Nature. 2014 Dec 1. doi: 10.1038/nature13950. PMID:25470061<ref>PMID:25470061</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:13, 17 December 2014
Cryo-EM structure of ryanodine receptor/Calstabin-2 complex
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Categories: Oryctolagus cuniculus | Peptidylprolyl isomerase | Clarke, O B | Frank, J | Georges, A des | Grassucci, R A | Hendrickson, W A | Mancia, F | Marks, A R | Reiken, S | Zalk, R | Alpha solenoid scaffold | Calcium release | Calstabin | Closed-state | Ef-hand | Excitation-contraction coupling in muscle | Fkbp12 | Six-transmembrane ion channel | Spry | Transport protein-isomerase complex
