2l5y

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[[Image:2l5y.png|left|200px]]
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==NMR structure of calcium-loaded STIM2 EF-SAM.==
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<StructureSection load='2l5y' size='340' side='right' caption='[[2l5y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2l5y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L5Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA1482, STIM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2l5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l5y RCSB], [http://www.ebi.ac.uk/pdbsum/2l5y PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Stromal interaction molecules (STIM)s function as endoplasmic reticulum calcium (Ca(2+)) sensors that differentially regulate plasma membrane Ca(2+) release activated Ca(2+) channels in various cells. To probe the structural basis for the functional differences between STIM1 and STIM2 we engineered a series of EF-hand and sterile alpha motif (SAM) domain (EF-SAM) chimeras, demonstrating that the STIM1 Ca(2+)-binding EF-hand and the STIM2 SAM domain are major contributors to the autoinhibition of oligomerization in each respective isoform. Our nuclear magnetic resonance (NMR) derived STIM2 EF-SAM structure provides a rationale for an augmented stability, which involves a 54 degrees pivot in the EF-hand:SAM domain orientation permissible by an expanded nonpolar cleft, ionic interactions, and an enhanced hydrophobic SAM core, unique to STIM2. Live cells expressing "super-unstable" or "super-stable" STIM1/STIM2 EF-SAM chimeras in the full-length context show a remarkable correlation with the in vitro data. Together, our data suggest that divergent Ca(2+)- and SAM-dependent stabilization of the EF-SAM fold contributes to the disparate regulation of store-operated Ca(2+) entry by STIM1 and STIM2.
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{{STRUCTURE_2l5y| PDB=2l5y | SCENE= }}
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Auto-inhibitory role of the EF-SAM domain of STIM proteins in store-operated calcium entry.,Zheng L, Stathopulos PB, Schindl R, Li GY, Romanin C, Ikura M Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1337-42. Epub 2011 Jan 7. PMID:21217057<ref>PMID:21217057</ref>
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===NMR structure of calcium-loaded STIM2 EF-SAM.===
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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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{{ABSTRACT_PUBMED_21217057}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2l5y]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5Y OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:021217057</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ikura, M.]]
[[Category: Ikura, M.]]

Revision as of 11:22, 20 October 2014

NMR structure of calcium-loaded STIM2 EF-SAM.

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