7m6a
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ==== | + | ==High resolution structure of the membrane embedded skeletal muscle ryanodine receptor== |
| - | <StructureSection load='7m6a' size='340' side='right'caption='[[7m6a]]' scene=''> | + | <StructureSection load='7m6a' size='340' side='right'caption='[[7m6a]], [[Resolution|resolution]] 3.36Å' 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'>[[7m6a]] 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=7M6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M6A 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=7m6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m6a OCA], [https://pdbe.org/7m6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m6a RCSB], [https://www.ebi.ac.uk/pdbsum/7m6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m6a ProSAT]</span></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]] 3.36Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7m6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m6a OCA], [https://pdbe.org/7m6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m6a RCSB], [https://www.ebi.ac.uk/pdbsum/7m6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m6a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [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 type 1 ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is required for skeletal muscle excitation-contraction coupling and is the largest known ion channel, composed of four 565-kDa protomers. Cryogenic electron microscopy (cryo-EM) studies of the RyR have primarily used detergent to solubilize the channel; in the present study, we have used cryo-EM to solve high-resolution structures of the channel in liposomes using a gel-filtration approach with on-column detergent removal to form liposomes and incorporate the channel simultaneously. This allowed us to resolve the structure of the channel in the primed and open states at 3.4 and 4.0 A, respectively, with a single dataset. This method offers validation for detergent-based structures of the RyR and offers a starting point for utilizing a chemical gradient mimicking the SR, where Ca(2+) concentrations are millimolar in the lumen and nanomolar in the cytosol. | ||
| + | |||
| + | High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor.,Melville Z, Kim K, Clarke OB, Marks AR Structure. 2022 Jan 6;30(1):172-180.e3. doi: 10.1016/j.str.2021.08.001. Epub 2021 , Aug 31. PMID:34469755<ref>PMID:34469755</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7m6a" 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: Z | + | [[Category: Oryctolagus cuniculus]] |
| + | [[Category: Clarke OB]] | ||
| + | [[Category: Kim K]] | ||
| + | [[Category: Marks AR]] | ||
| + | [[Category: Melville Z]] | ||
Current revision
High resolution structure of the membrane embedded skeletal muscle ryanodine receptor
| |||||||||||
