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The high-resolution crystal structure of phosphatidylinositol 4-kinase IIβ and the crystal structure of phosphatidylinositol 4-kinase IIα containing a nucleoside analogue provide a structural basis for isoform-specific inhibitor design
M. Klima, A. Baumlova, D. Chalupska, H. Hřebabecký, M. Dejmek, R. Nencka, E. Boura,
Acta crystallographica. Section D, Biological crystallography.
2015 ;
71 (Pt 7) :
1555-63. (Biological crystallography)
[pub] 20150630
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
Perzistentní odkaz
https://www.medvik.cz/link/bmc16020587
- MeSH
- 1-fosfatidylinositol-4-kinasa antagonisté a inhibitory chemie metabolismus MeSH
- adenosintrifosfát metabolismus MeSH
- hydrofobní a hydrofilní interakce MeSH
- inhibitory proteinkinas chemie farmakologie MeSH
- katalytická doména MeSH
- konformace proteinů MeSH
- krystalografie rentgenová MeSH
- lidé MeSH
- nukleosidy chemie farmakologie MeSH
- protein - isoformy antagonisté a inhibitory chemie metabolismus MeSH
- racionální návrh léčiv * MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Phosphatidylinositol 4-phosphate (PI4P) is the most abundant monophosphoinositide in eukaryotic cells. Humans have four phosphatidylinositol 4-kinases (PI4Ks) that synthesize PI4P, among which are PI4K IIβ and PI4K IIα. In this study, two crystal structures are presented: the structure of human PI4K IIβ and the structure of PI4K IIα containing a nucleoside analogue. The former, a complex with ATP, is the first high-resolution (1.9 Å) structure of a PI4K. These structures reveal new details such as high conformational heterogeneity of the lateral hydrophobic pocket of the C-lobe and together provide a structural basis for isoform-specific inhibitor design.
Citace poskytuje Crossref.org
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