4WAE
Phosphatidylinositol 4-kinase III beta crystallized with ATP
Summary for 4WAE
| Entry DOI | 10.2210/pdb4wae/pdb |
| Descriptor | Phosphatidylinositol 4-kinase beta,Phosphatidylinositol 4-kinase beta, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | transferase |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Endomembrane system: Q9UBF8 |
| Total number of polymer chains | 1 |
| Total formula weight | 65771.95 |
| Authors | Chalupska, D.,Boura, E. (deposition date: 2014-08-29, release date: 2015-05-20, Last modification date: 2024-01-10) |
| Primary citation | Mejdrova, I.,Chalupska, D.,Kogler, M.,Sala, M.,Plackova, P.,Baumlova, A.,Hrebabecky, H.,Prochazkova, E.,Dejmek, M.,Guillon, R.,Strunin, D.,Weber, J.,Lee, G.,Birkus, G.,Mertlikova-Kaiserova, H.,Boura, E.,Nencka, R. Highly Selective Phosphatidylinositol 4-Kinase III beta Inhibitors and Structural Insight into Their Mode of Action. J.Med.Chem., 58:3767-3793, 2015 Cited by PubMed Abstract: Phosphatidylinositol 4-kinase IIIβ is a cellular lipid kinase pivotal to pathogenesis of various RNA viruses. These viruses hijack the enzyme in order to modify the structure of intracellular membranes and use them for the construction of functional replication machinery. Selective inhibitors of this enzyme are potential broad-spectrum antiviral agents, as inhibition of this enzyme results in the arrest of replication of PI4K IIIβ-dependent viruses. Herein, we report a detailed study of novel selective inhibitors of PI4K IIIβ, which exert antiviral activity against a panel of single-stranded positive-sense RNA viruses. Our crystallographic data show that the inhibitors occupy the binding site for the adenine ring of the ATP molecule and therefore prevent the phosphorylation reaction. PubMed: 25897704DOI: 10.1021/acs.jmedchem.5b00499 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.318 Å) |
Structure validation
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