5j8h
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of calmodulin in a complex with a peptide derived from a calmodulin-dependent kinase== | |
| + | <StructureSection load='5j8h' size='340' side='right' caption='[[5j8h]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5j8h]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J8H FirstGlance]. <br> | ||
| + | </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> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Elongation_factor_2]_kinase [Elongation factor 2] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.20 2.7.11.20] </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=5j8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8h OCA], [http://pdbe.org/5j8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8h RCSB], [http://www.ebi.ac.uk/pdbsum/5j8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/EF2K_HUMAN EF2K_HUMAN]] Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.<ref>PMID:14709557</ref> <ref>PMID:9144159</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Binding of Ca2+-loaded calmodulin (CaM) activates eukaryotic elongation factor 2 kinase (eEF-2K) that phosphorylates eEF-2, its only known cellular target, leading to a decrease in global protein synthesis. Here, using an eEF-2K-derived peptide (eEF-2KCBD) that encodes the region necessary for its CaM-mediated activation, we provide a structural basis for their interaction. The striking feature of this association is the absence of Ca2+ from the CaM C-lobe sites, even under high Ca2+ conditions. eEF-2KCBD engages CaM largely through the C lobe of the latter in an anti-parallel 1-5-8 hydrophobic mode reinforced by a pair of unique electrostatic contacts. Sparse interactions of eEF-2KCBD with the CaM N lobe results in persisting inter-lobe mobility. A conserved eEF-2K residue (W85) anchors it to CaM by inserting into a deep hydrophobic cavity within the CaM C lobe. Mutation of this residue (W85S) substantially weakens interactions between full-length eEF-2K and CaM in vitro and reduces eEF-2 phosphorylation in cells. | ||
| - | + | Structural Basis for the Recognition of Eukaryotic Elongation Factor 2 Kinase by Calmodulin.,Lee K, Alphonse S, Piserchio A, Tavares CD, Giles DH, Wellmann RM, Dalby KN, Ghose R Structure. 2016 Sep 6;24(9):1441-1451. doi: 10.1016/j.str.2016.06.015. Epub 2016 , Aug 4. PMID:27499441<ref>PMID:27499441</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5j8h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alphonse, S]] | ||
| + | [[Category: Dalby, K N]] | ||
| + | [[Category: Ghose, R]] | ||
| + | [[Category: Giles, D H]] | ||
| + | [[Category: Lee, K]] | ||
| + | [[Category: Piserchio, A]] | ||
| + | [[Category: Tavares, C D.J]] | ||
| + | [[Category: Wellmann, R M]] | ||
| + | [[Category: Calmodulin eef2k complex kinase]] | ||
| + | [[Category: Metal binding protein-transferase complex]] | ||
Revision as of 21:08, 10 September 2016
Structure of calmodulin in a complex with a peptide derived from a calmodulin-dependent kinase
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