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| - | | + | #REDIRECT [[5lvz]] This PDB entry is obsolete and replaced by 5lvz |
| - | ==Crystal structure of yeast 14-3-3 protein (Bmh1) from Lachancea thermotolerans==
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| - | <StructureSection load='5lho' size='340' side='right' caption='[[5lho]], [[Resolution|resolution]] 1.95Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5lho]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHO FirstGlance]. <br>
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| - | </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=5lho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lho OCA], [http://pdbe.org/5lho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lho RCSB], [http://www.ebi.ac.uk/pdbsum/5lho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lho ProSAT]</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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| - | 14-3-3 proteins bind phosphorylated binding partners to regulate several of their properties, including enzymatic activity, stability and subcellular localization. Here, two crystal structures are presented: the crystal structures of the 14-3-3 protein (also known as Bmh1) from the yeast Lachancea thermotolerans in the unliganded form and bound to a phosphopeptide derived from human PI4KB (phosphatidylinositol 4-kinase B). The structures demonstrate the high evolutionary conservation of ligand recognition by 14-3-3 proteins. The structural analysis suggests that ligand recognition by 14-3-3 proteins evolved very early in the evolution of eukaryotes and remained conserved, underlying the importance of 14-3-3 proteins in physiology.
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| - | Crystal structures of a yeast 14-3-3 protein from Lachancea thermotolerans in the unliganded form and bound to a human lipid kinase PI4KB-derived peptide reveal high evolutionary conservation.,Eisenreichova A, Klima M, Boura E Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):799-803. Epub 2016, Oct 24. PMID:27827352<ref>PMID:27827352</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5lho" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Boura, E]]
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| - | [[Category: Klima, M]]
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| - | [[Category: 14-3-3]]
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| - | [[Category: Bmh1]]
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| - | [[Category: Signaling protein]]
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