8duj

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8duj]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Pandinus_imperator Pandinus imperator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DUJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[8duj]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Pandinus_imperator Pandinus imperator]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DUJ 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=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>
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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]] 3.7&#8491;</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=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=8duj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8duj OCA], [https://pdbe.org/8duj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8duj RCSB], [https://www.ebi.ac.uk/pdbsum/8duj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8duj ProSAT]</span></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=8duj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8duj OCA], [https://pdbe.org/8duj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8duj RCSB], [https://www.ebi.ac.uk/pdbsum/8duj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8duj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/CAIMP_PANIM CAIMP_PANIM] This toxin affects the activity of ryanodine receptors 1, 2 and 3 (RyR1, RyR2 and RyR3) (PubMed:1334561, PubMed:9565405, PubMed:11867448). At lower concentrations the toxin increases full openings of the RyRs, and at higher concentrations it inhibits full openings and induces openings to subconductance levels (30% of the full conductance state) and reduces the number of full conductance openings (PubMed:9565405, PubMed:27114612). The different actions may be attributed to the toxins binding at different sites on the RyRs, with binding at a high-affinity site mediating the increase in full openings and the induction of subconductance states evoked upon binding to a lower-affinity site (PubMed:14699105). Furthermore, it triggers calcium release from sarcoplasmic vesicles (11.7 nM are enough to induce a sharp release, and 70% of the total calcium is released after toxin (100 nM) addition) probably by acting as a cell-penetrating peptide (CPP) (PubMed:1334561, PubMed:27114612). In addition, it has been shown to dose-dependently stimulate ryanodine binding to RyR1 (EC(50)=8.7 nM) (PubMed:27114612). It also augments the bell-shaped calcium-[3H]ryanodine binding curve that is maximal at about 10 uM calcium concentration (PubMed:27114612). It binds a different site as ryanodine (PubMed:9565405). It acts synergistically with caffeine (By similarity). In vivo, intracerebroventricular injection into mice induces neurotoxic symptoms, followed by death (By similarity).[UniProtKB:A0A1L4BJ42][UniProtKB:B8QG00][UniProtKB:P60254]<ref>PMID:11867448</ref> <ref>PMID:1334561</ref> <ref>PMID:14699105</ref> <ref>PMID:9565405</ref>
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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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Calcins are peptides from scorpion venom with the unique ability to cross cell membranes, gaining access to intracellular targets. Ryanodine Receptors (RyR) are intracellular ion channels that control release of Ca(2+) from the endoplasmic and sarcoplasmic reticulum. Calcins target RyRs and induce long-lived subconductance states, whereby single-channel currents are decreased. We used cryo-electron microscopy to reveal the binding and structural effects of imperacalcin, showing that it opens the channel pore and causes large asymmetry throughout the cytosolic assembly of the tetrameric RyR. This also creates multiple extended ion conduction pathways beyond the transmembrane region, resulting in subconductance. Phosphorylation of imperacalcin by protein kinase A prevents its binding to RyR through direct steric hindrance, showing how posttranslational modifications made by the host organism can determine the fate of a natural toxin. The structure provides a direct template for developing calcin analogs that result in full channel block, with potential to treat RyR-related disorders.
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Cryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals subconductance that is abolished by PKA phosphorylation.,Haji-Ghassemi O, Chen YS, Woll K, Gurrola GB, Valdivia CR, Cai W, Li S, Valdivia HH, Van Petegem F Sci Adv. 2023 May 24;9(21):eadf4936. doi: 10.1126/sciadv.adf4936. Epub 2023 May , 24. PMID:37224245<ref>PMID:37224245</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8duj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>

Current revision

Global map in C1 of RyR1 particles in complex with ImperaCalcin

PDB ID 8duj

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