3ter: Difference between revisions
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==Crystal structure of SOAR domain with Inhibition helix from C. elegans== | ==Crystal structure of SOAR domain with Inhibition helix from C. elegans== | ||
<StructureSection load='3ter' size='340' side='right' caption='[[3ter]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='3ter' size='340' side='right' caption='[[3ter]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ter]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ter]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TER FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stim-1, Y55B1BM.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">stim-1, Y55B1BM.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | ||
<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=3ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ter OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ter RCSB], [http://www.ebi.ac.uk/pdbsum/3ter PDBsum]</span></td></tr> | <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=3ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ter OCA], [http://pdbe.org/3ter PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ter RCSB], [http://www.ebi.ac.uk/pdbsum/3ter PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ter ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3ter" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Caeel]] | ||
[[Category: Cai, X]] | [[Category: Cai, X]] | ||
[[Category: Jin, H]] | [[Category: Jin, H]] | ||
Revision as of 17:20, 4 August 2016
Crystal structure of SOAR domain with Inhibition helix from C. elegansCrystal structure of SOAR domain with Inhibition helix from C. elegans
Structural highlights
Publication Abstract from PubMedCalcium influx through the Ca(2+) release-activated Ca(2+) (CRAC) channel is an essential process in many types of cells. Upon store depletion, the calcium sensor in the endoplasmic reticulum, STIM1, activates Orai1, a CRAC channel in the plasma membrane. We have determined the structures of SOAR from Homo sapiens (hSOAR), which is part of STIM1 and is capable of constitutively activating Orai1, and the entire coiled coil region of STIM1 from Caenorhabditis elegans (ceSTIM1-CCR) in an inactive state. Our studies reveal that the formation of a SOAR dimer is necessary to activate the Orai1 channel. Mutations that disrupt SOAR dimerization or remove the cluster of positive residues abolish STIM1 activation of Orai1. We identified a possible inhibitory helix within the structure of ceSTIM1-CCR that tightly interacts with SOAR. Functional studies suggest that the inhibitory helix may keep the C-terminus of STIM1 in an inactive state. Our data allowed us to propose a model for STIM1 activation. Structural and mechanistic insights into the activation of Stromal interaction molecule 1 (STIM1).,Yang X, Jin H, Cai X, Li S, Shen Y Proc Natl Acad Sci U S A. 2012 Mar 26. PMID:22451904[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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