7t3p

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Current revision (06:48, 21 November 2024) (edit) (undo)
 
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<StructureSection load='7t3p' size='340' side='right'caption='[[7t3p]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='7t3p' size='340' side='right'caption='[[7t3p]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7t3p]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T3P FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T3P 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=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</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]] 3.2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</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=7t3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t3p OCA], [https://pdbe.org/7t3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t3p RCSB], [https://www.ebi.ac.uk/pdbsum/7t3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t3p 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=7t3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t3p OCA], [https://pdbe.org/7t3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t3p RCSB], [https://www.ebi.ac.uk/pdbsum/7t3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t3p ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[[https://www.uniprot.org/uniprot/ITPR3_HUMAN ITPR3_HUMAN]] Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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A pivotal component of the calcium (Ca(2+)) signaling toolbox in cells is the inositol 1,4,5-triphosphate (IP3) receptor (IP3R), which mediates Ca(2+) release from the endoplasmic reticulum (ER), controlling cytoplasmic and organellar Ca(2+) concentrations. IP3Rs are co-activated by IP3 and Ca(2+), inhibited by Ca(2+) at high concentrations, and potentiated by ATP. However, the underlying molecular mechanisms are unclear. Here we report cryo-electron microscopy (cryo-EM) structures of human type-3 IP3R obtained from a single dataset in multiple gating conformations: IP3-ATP bound pre-active states with closed channels, IP3-ATP-Ca(2+) bound active state with an open channel, and IP3-ATP-Ca(2+) bound inactive state with a closed channel. The structures demonstrate how IP3-induced conformational changes prime the receptor for activation by Ca(2+), how Ca(2+) binding leads to channel opening, and how ATP modulates the activity, providing insights into the long-sought questions regarding the molecular mechanism underpinning receptor activation and gating.
 
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Structural basis for activation and gating of IP3 receptors.,Schmitz EA, Takahashi H, Karakas E Nat Commun. 2022 Mar 17;13(1):1408. doi: 10.1038/s41467-022-29073-2. PMID:35301323<ref>PMID:35301323</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 7t3p" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Karakas, E]]
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[[Category: Karakas E]]
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[[Category: Schmitz, E A]]
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[[Category: Schmitz EA]]
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[[Category: Takahashi, H]]
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[[Category: Takahashi H]]
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[[Category: Calcium signaling]]
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[[Category: Ip3 receptor]]
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[[Category: Metal transport]]
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Current revision

IP3 and ATP bound type 3 IP3 receptor in the pre-active A state

PDB ID 7t3p

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