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
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
PubMed
27827352
PubMed Central
PMC5101580
DOI
10.1107/s2053230x16015053
PII: S2053230X16015053
Knihovny.cz E-zdroje
- Klíčová slova
- 14-3-3 proteins, Bmh1, Bmh2, Lachancea thermotolerans, PI4KB, crystal structure, phosphopeptide,
- MeSH
- 1-fosfatidylinositol-4-kinasa chemie genetika metabolismus MeSH
- Escherichia coli genetika metabolismus MeSH
- exprese genu MeSH
- fosfoproteiny chemie genetika metabolismus MeSH
- fungální proteiny chemie genetika metabolismus MeSH
- klonování DNA MeSH
- konformace proteinů, alfa-helix MeSH
- konzervovaná sekvence MeSH
- krystalografie rentgenová MeSH
- lidé MeSH
- ligandy MeSH
- molekulární evoluce MeSH
- molekulární modely MeSH
- plazmidy chemie metabolismus MeSH
- protein - isoformy chemie genetika metabolismus MeSH
- proteiny 14-3-3 chemie genetika metabolismus MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- Saccharomycetales chemie metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- strukturní homologie proteinů MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 1-fosfatidylinositol-4-kinasa MeSH
- fosfoproteiny MeSH
- fungální proteiny MeSH
- ligandy MeSH
- protein - isoformy MeSH
- proteiny 14-3-3 MeSH
- rekombinantní proteiny MeSH
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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