4o9b

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Current revision (12:38, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o9b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ioz 4ioz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9B FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o9b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ioz 4ioz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9B 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=CD:CADMIUM+ION'>CD</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">X-ray diffraction, [[Resolution|Resolution]] 2.604&#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=CD:CADMIUM+ION'>CD</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=4o9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9b OCA], [https://pdbe.org/4o9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9b RCSB], [https://www.ebi.ac.uk/pdbsum/4o9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9b 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=4o9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9b OCA], [https://pdbe.org/4o9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9b RCSB], [https://www.ebi.ac.uk/pdbsum/4o9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9b ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/STIM1_HUMAN STIM1_HUMAN] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1.<ref>PMID:9377559</ref> <ref>PMID:16005298</ref> <ref>PMID:15866891</ref> <ref>PMID:16208375</ref> <ref>PMID:16807233</ref> <ref>PMID:16766533</ref> <ref>PMID:16733527</ref> <ref>PMID:16537481</ref> <ref>PMID:22464749</ref>
[https://www.uniprot.org/uniprot/STIM1_HUMAN STIM1_HUMAN] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1.<ref>PMID:9377559</ref> <ref>PMID:16005298</ref> <ref>PMID:15866891</ref> <ref>PMID:16208375</ref> <ref>PMID:16807233</ref> <ref>PMID:16766533</ref> <ref>PMID:16733527</ref> <ref>PMID:16537481</ref> <ref>PMID:22464749</ref>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Store-operated Ca(2+) entry (SOCE) is a critical Ca(2+) signaling pathway in many cell types. After sensing Ca(2+) store depletion in the endoplasmic reticulum (ER) lumen, STIM1 (STromal Interaction Molecule 1) oligomerizes and then interacts with and activates the Orai1 calcium channel. Our previous research has demonstrated that the inhibitory helix (IH) adjacent to the first coiled-coil region (CC1) of STIM1 may keep the whole C-terminus of STIM1 in an inactive state. However, the specific conformational change of CC1-IH that drives the transition of STIM1 from the resting state to the active state remains elusive. Herein, we report the structural analysis of CC1-IH, which revealed that the entire CC1-IH molecule forms a very long helix. Structural and biochemical analyses indicated that IH, and not the CC1 region, contributes to the oligomerization of STIM1. Small-angle X-ray scattering (SAXS) analysis suggested that the C-terminus of STIM1 including the IH region displays a collapsed conformation, whereas the construct without the IH region has an extended conformation. These two conformations may correspond to the conformational states of the C-terminus of STIM1 before and after activation. Taken together, our results provide direct biochemical evidence that the IH region controls the conformational switching of the C-terminus of STIM1.
 
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The Inhibitory Helix Controls the Intramolecular Conformational Switching of the C-Terminus of STIM1.,Cui B, Yang X, Li S, Lin Z, Wang Z, Dong C, Shen Y PLoS One. 2013 Sep 19;8(9):e74735. doi: 10.1371/journal.pone.0074735. PMID:24069340<ref>PMID:24069340</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 4o9b" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

The Structure of CC1-IH in human STIM1.

PDB ID 4o9b

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