The crystal structure of the phosphatidylinositol 4-kinase II alpha

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00435136" target="_blank" >RIV/61388963:_____/14:00435136 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.15252/embr.201438841" target="_blank" >http://dx.doi.org/10.15252/embr.201438841</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.15252/embr.201438841" target="_blank" >10.15252/embr.201438841</a>

Result language
angličtina
Original language name
The crystal structure of the phosphatidylinositol 4-kinase II alpha
Original language description
Phosphoinositides are a class of phospholipids generated by the action of phosphoinositide kinases with key regulatory functions in eukaryotic cells. Here, we present the atomic structure of phosphatidylinositol 4-kinase type II alpha (PI4K II alpha), incomplex with ATP solved by X-ray crystallography at 2.8 angstrom resolution. The structure revealed a non-typical kinase fold that could be divided into Nand C-lobes with the ATP binding groove located in between. Surprisingly, a second ATP was found ina lateral hydrophobic pocket of the C-lobe. Molecular simulations and mutagenesis analysis revealed the membrane binding mode and the putative function of the hydrophobic pocket. Taken together, our results suggest a mechanism of PI4K II alpha recruitment, regulation, and function at the membrane.
Czech name
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Czech description
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Type
J<sub>x</sub> - 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
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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