5jol
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Calcium-free EF-hand domain of L-plastin== | |
| + | <StructureSection load='5jol' size='340' side='right' caption='[[5jol]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jol]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JOL FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5joj|5joj]]</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=5jol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jol OCA], [http://pdbe.org/5jol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jol RCSB], [http://www.ebi.ac.uk/pdbsum/5jol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jol ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PLSL_HUMAN PLSL_HUMAN]] Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69.<ref>PMID:16636079</ref> <ref>PMID:17294403</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | L-plastin is a calcium-regulated actin-bundling protein that is expressed in cells of hematopoietic origin and in most metastatic cancer cells. These cell types are mobile and require the constant remodeling of their actin cytoskeleton, where L-plastin bundles filamentous actin. The calcium-dependent regulation of the actin-bundling activity of L-plastin is not well understood. We have used NMR spectroscopy to determine the solution structure of the EF-hand calcium-sensor headpiece domain. Unexpectedly, this domain does not bind directly to the four CH-domains of L-plastin. A novel switch helix is present immediately after the calcium-binding region and it binds tightly to the EF-hand motifs in the presence of calcium. We demonstrate that this switch helix plays a major role during actin-bundling. Moreover a peptide that competitively inhibits the association between the EF-hand motifs and the switch helix was shown to deregulate the actin-bundling activity of L-plastin. Overall, these findings may help to develop new drugs that target the L-plastin headpiece and interfere in the metastatic activity of cancer cells. | ||
| - | + | The Calcium-Dependent Switch Helix of L-Plastin Regulates Actin Bundling.,Ishida H, Jensen KV, Woodman AG, Hyndman ME, Vogel HJ Sci Rep. 2017 Feb 1;7:40662. doi: 10.1038/srep40662. PMID:28145401<ref>PMID:28145401</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5jol" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hyndman, M E]] | ||
| + | [[Category: Ishida, H]] | ||
| + | [[Category: Jensen, K V]] | ||
| + | [[Category: Vogel, H J]] | ||
| + | [[Category: Woodman, A G]] | ||
| + | [[Category: Calcium-binding]] | ||
| + | [[Category: Ef-hand]] | ||
| + | [[Category: L-plastin]] | ||
| + | [[Category: Metal binding protein]] | ||
Revision as of 12:58, 19 April 2017
Calcium-free EF-hand domain of L-plastin
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