View source for 4wae


==Phosphatidylinositol 4-kinase III beta crystallized with ATP==
<StructureSection load='4wae' size='340' side='right'caption='[[4wae]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wae]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WAE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.318&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wae OCA], [https://pdbe.org/4wae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wae RCSB], [https://www.ebi.ac.uk/pdbsum/4wae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wae ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PI4KB_HUMAN PI4KB_HUMAN] Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity).<ref>PMID:9405935</ref> <ref>PMID:10559940</ref> <ref>PMID:12749687</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phosphatidylinositol 4-kinase IIIbeta 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 IIIbeta-dependent viruses. Herein, we report a detailed study of novel selective inhibitors of PI4K IIIbeta, 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.

Highly Selective Phosphatidylinositol 4-Kinase IIIbeta Inhibitors and Structural Insight into Their Mode of Action.,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 J Med Chem. 2015 May 14;58(9):3767-93. doi: 10.1021/acs.jmedchem.5b00499. Epub, 2015 May 4. PMID:25897704<ref>PMID:25897704</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wae" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phosphatidylinositol 4-kinase|Phosphatidylinositol 4-kinase]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Boura E]]
[[Category: Chalupska D]]