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6jhn

From Proteopedia

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Current revision (10:38, 27 March 2024) (edit) (undo)
 
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<SX load='6jhn' size='340' side='right' viewer='molstar' caption='[[6jhn]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
<SX load='6jhn' size='340' side='right' viewer='molstar' caption='[[6jhn]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jhn]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=6JHN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JHN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jhn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JHN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jhn OCA], [https://pdbe.org/6jhn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jhn RCSB], [https://www.ebi.ac.uk/pdbsum/6jhn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jhn ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jhn OCA], [http://pdbe.org/6jhn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jhn RCSB], [http://www.ebi.ac.uk/pdbsum/6jhn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jhn ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The type 2 ryanodine receptor (RyR2) is responsible for releasing Ca(2+) from the sarcoplasmic reticulum of cardiomyocytes, subsequently leading to muscle contraction. Here, we report 4 cryo-electron microscopy (cryo-EM) structures of porcine RyR2 bound to distinct modulators that, together with our published structures, provide mechanistic insight into RyR2 regulation. Ca(2+) alone induces a contraction of the central domain that facilitates the dilation of the S6 bundle but is insufficient to open the pore. The small-molecule agonist PCB95 helps Ca(2+) to overcome the barrier for opening. FKBP12.6 induces a relaxation of the central domain that decouples it from the S6 bundle, stabilizing RyR2 in a closed state even in the presence of Ca(2+) and PCB95. Although the channel is open when PCB95 is replaced by caffeine and adenosine 5'-triphosphate (ATP), neither of the modulators alone can sufficiently counter the antagonistic effect to open the channel. Our study marks an important step toward mechanistic understanding of the sophisticated regulation of this key channel whose aberrant activity engenders life-threatening cardiac disorders.
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Molecular basis for allosteric regulation of the type 2 ryanodine receptor channel gating by key modulators.,Chi X, Gong D, Ren K, Zhou G, Huang G, Lei J, Zhou Q, Yan N Proc Natl Acad Sci U S A. 2019 Dec 2. pii: 1914451116. doi:, 10.1073/pnas.1914451116. PMID:31792195<ref>PMID:31792195</ref>
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==See Also==
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*[[FKBP 3D structures|FKBP 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]]
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</div>
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<div class="pdbe-citations 6jhn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
 
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Chi, X M]]
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[[Category: Chi XM]]
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[[Category: Gong, D S]]
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[[Category: Gong DS]]
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[[Category: Huang, G X.Y]]
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[[Category: Huang GXY]]
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[[Category: Lei, J L]]
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[[Category: Lei JL]]
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[[Category: Ren, K]]
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[[Category: Ren K]]
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[[Category: Yan, N]]
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[[Category: Yan N]]
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[[Category: Zhou, G W]]
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[[Category: Zhou GW]]
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[[Category: Zhou, Q]]
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[[Category: Zhou Q]]
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[[Category: Cryo-em]]
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[[Category: Membrane protein]]
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Current revision

Structure of RyR2 (F/C/Ca2+ dataset)

6jhn, resolution 4.50Å

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