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The crystal structure of the phosphatidylinositol 4-kinase IIα

A. Baumlova, D. Chalupska, B. Róźycki, M. Jovic, E. Wisniewski, M. Klima, A. Dubankova, DP. Kloer, R. Nencka, T. Balla, E. Boura,

. 2014 ; 15 (10) : 1085-92.

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc15023079
E-zdroje Online Plný text

NLK Free Medical Journals od 2000 do Před 1 rokem
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Odkazy

PubMed 25168678
DOI 10.15252/embr.201438841
Knihovny.cz E-zdroje

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 IIα (PI4K IIα), in complex with ATP solved by X-ray crystallography at 2.8 Å resolution. The structure revealed a non-typical kinase fold that could be divided into N- and C-lobes with the ATP binding groove located in between. Surprisingly, a second ATP was found in a 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 IIα recruitment, regulation, and function at the membrane.

Citace poskytuje Crossref.org

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