期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 72, 期 -, 页码 799-803出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X16015053
关键词
14-3-3 proteins; Bmh1; Bmh2; crystal structure; phosphopeptide; PI4KB; Lachancea thermotolerans
资金
- Project InterBioMed from Ministry of Education of the Czech Republic [LO1302]
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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