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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00466860" target="_blank" >RIV/61388963:_____/16:00466860 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1107/S2053230X16015053" target="_blank" >http://dx.doi.org/10.1107/S2053230X16015053</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2053230X16015053" target="_blank" >10.1107/S2053230X16015053</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

—

Project

<a href="/en/project/LO1302" target="_blank" >LO1302: InterBioMed</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS

ISSN

2053-230X

e-ISSN

—

Volume of the periodical

72

Issue of the periodical within the volume

11

Country of publishing house

GB - UNITED KINGDOM

Number of pages

5

Pages from-to

799-803

UT code for WoS article

000387585800001

EID of the result in the Scopus database

2-s2.0-84994718361