5xa0

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==Crystal structure of inositol 1,4,5-trisphosphate receptor cytosolic domain==
==Crystal structure of inositol 1,4,5-trisphosphate receptor cytosolic domain==
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<StructureSection load='5xa0' size='340' side='right' caption='[[5xa0]], [[Resolution|resolution]] 5.81&Aring;' scene=''>
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<StructureSection load='5xa0' size='340' side='right'caption='[[5xa0]], [[Resolution|resolution]] 5.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xa0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XA0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xa0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XA0 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x9z|5x9z]], [[5xa1|5xa1]]</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">X-ray diffraction, [[Resolution|Resolution]] 5.812&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xa0 OCA], [http://pdbe.org/5xa0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xa0 RCSB], [http://www.ebi.ac.uk/pdbsum/5xa0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xa0 ProSAT]</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=5xa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xa0 OCA], [https://pdbe.org/5xa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xa0 RCSB], [https://www.ebi.ac.uk/pdbsum/5xa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xa0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ITPR1_MOUSE ITPR1_MOUSE]] Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways.<ref>PMID:2554142</ref> <ref>PMID:19752026</ref> <ref>PMID:20813840</ref>
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[https://www.uniprot.org/uniprot/ITPR1_MOUSE ITPR1_MOUSE] Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways.<ref>PMID:2554142</ref> <ref>PMID:19752026</ref> <ref>PMID:20813840</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The inositol 1,4,5-trisphosphate (IP3) receptor (IP3R) is an IP3-gated ion channel that releases calcium ions (Ca2+) from the endoplasmic reticulum. The IP3-binding sites in the large cytosolic domain are distant from the Ca2+ conducting pore, and the allosteric mechanism of how IP3 opens the Ca2+ channel remains elusive. Here, we identify a long-range gating mechanism uncovered by channel mutagenesis and X-ray crystallography of the large cytosolic domain of mouse type 1 IP3R in the absence and presence of IP3 Analyses of two distinct space group crystals uncovered an IP3-dependent global translocation of the curvature alpha-helical domain interfacing with the cytosolic and channel domains. Mutagenesis of the IP3R channel revealed an essential role of a leaflet structure in the alpha-helical domain. These results suggest that the curvature alpha-helical domain relays IP3-controlled global conformational dynamics to the channel through the leaflet, conferring long-range allosteric coupling from IP3 binding to the Ca2+ channel.
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IP3-mediated gating mechanism of the IP3 receptor revealed by mutagenesis and X-ray crystallography.,Hamada K, Miyatake H, Terauchi A, Mikoshiba K Proc Natl Acad Sci U S A. 2017 May 2;114(18):4661-4666. doi:, 10.1073/pnas.1701420114. Epub 2017 Apr 17. PMID:28416699<ref>PMID:28416699</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 5xa0" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Inositol 1%2C4%2C5-Trisphosphate Receptor|Inositol 1%2C4%2C5-Trisphosphate Receptor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hamada, K]]
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[[Category: Large Structures]]
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[[Category: Mikoshiba, K]]
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[[Category: Mus musculus]]
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[[Category: Miyatake, H]]
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[[Category: Hamada K]]
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[[Category: Terauchi, A]]
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[[Category: Mikoshiba K]]
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[[Category: Metal transport]]
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[[Category: Miyatake H]]
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[[Category: Receptor channel calcium]]
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[[Category: Terauchi A]]

Current revision

Crystal structure of inositol 1,4,5-trisphosphate receptor cytosolic domain

PDB ID 5xa0

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