View source for 6mu1


==Structure of full-length IP3R1 channel bound with Adenophostin A==
<SX load='6mu1' size='340' side='right' viewer='molstar' caption='[[6mu1]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mu1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MU1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JYP:[(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-(hydroxymethyl)-4-[(2~{R},3~{S},4~{R},5~{S},6~{S})-6-(hydroxymethyl)-3-oxidanyl-4,5-diphosphonooxy-oxan-2-yl]oxy-oxolan-3-yl]+dihydrogen+phosphate'>JYP</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=6mu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mu1 OCA], [https://pdbe.org/6mu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mu1 RCSB], [https://www.ebi.ac.uk/pdbsum/6mu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mu1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ITPR1_RAT ITPR1_RAT] 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 (By similarity).
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== Publication Abstract from PubMed ==
Inositol-1,4,5-trisphosphate receptors (InsP3Rs) are cation channels that mobilize Ca(2+) from intracellular stores in response to a wide range of cellular stimuli. The paradigm of InsP3R activation is the coupled interplay between binding of InsP3 and Ca(2+) that switches the ion conduction pathway between closed and open states to enable the passage of Ca(2+) through the channel. However, the molecular mechanism of how the receptor senses and decodes ligand-binding signals into gating motion remains unknown. Here, we present the electron cryo-microscopy structure of InsP3R1 from rat cerebellum determined to 4.1 A resolution in the presence of activating concentrations of Ca(2+) and adenophostin A (AdA), a structural mimetic of InsP3 and the most potent known agonist of the channel. Comparison with the 3.9 A-resolution structure of InsP3R1 in the Apo-state, also reported herein, reveals the binding arrangement of AdA in the tetrameric channel assembly and striking ligand-induced conformational rearrangements within cytoplasmic domains coupled to the dilation of a hydrophobic constriction at the gate. Together, our results provide critical insights into the mechanistic principles by which ligand-binding allosterically gates InsP3R channel.

Cryo-EM reveals ligand induced allostery underlying InsP3R channel gating.,Fan G, Baker MR, Wang Z, Seryshev AB, Ludtke SJ, Baker ML, Serysheva II Cell Res. 2018 Nov 23. pii: 10.1038/s41422-018-0108-5. doi:, 10.1038/s41422-018-0108-5. PMID:30470765<ref>PMID:30470765</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6mu1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Inositol 1%2C4%2C5-Trisphosphate Receptor|Inositol 1%2C4%2C5-Trisphosphate Receptor]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Baker ML]]
[[Category: Baker MR]]
[[Category: Fan G]]
[[Category: Ludtke SJ]]
[[Category: Seryshev A]]
[[Category: Serysheva II]]
[[Category: Wang Z]]