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

0466860 - ÚOCHB 2017 RIV GB eng J - Journal Article
Eisenreichová, Andrea - Klíma, Martin - Bouřa, Evžen
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.
Acta Crystallographica Section F-Structural Biology Communications. Roč. 72, č. 11 (2016), s. 799-803. E-ISSN 2053-230X
R&D Projects: GA MŠMT LO1302
Institutional support: RVO:61388963
Keywords : 14-3-3 proteins * Bmh1 * Bmh2 * crystal structure * phosphopeptide
Subject RIV: CE - Biochemistry
Impact factor: 0.799, year: 2016

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.
Permanent Link: http://hdl.handle.net/11104/0265064