8dtb
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8dtb]] is a 5 chain structure with sequence from [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=8DTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DTB FirstGlance]. <br> | <table><tr><td colspan='2'>[[8dtb]] is a 5 chain structure with sequence from [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=8DTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DTB FirstGlance]. <br> | ||
| - | </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=CFF:CAFFEINE'>CFF</scene></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]] 3.14Å</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=CFF:CAFFEINE'>CFF</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=8dtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dtb OCA], [https://pdbe.org/8dtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dtb RCSB], [https://www.ebi.ac.uk/pdbsum/8dtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dtb 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=8dtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dtb OCA], [https://pdbe.org/8dtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dtb RCSB], [https://www.ebi.ac.uk/pdbsum/8dtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dtb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | [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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| + | ==See Also== | ||
| + | *[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Focus/local refined map in C1 of signal subtracted RyR1 particles in complex with ImperaCalcin
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