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 - Článek v odborném periodiku
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
Grant CEP: GA MŠMT LO1302
Institucionální podpora: RVO:61388963
Klíčová slova: 14-3-3 proteins * Bmh1 * Bmh2 * crystal structure * phosphopeptide
Kód oboru RIV: CE - Biochemie
Impakt faktor: 0.799, rok: 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.
Trvalý link: http://hdl.handle.net/11104/0265064