4wtv
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4wtv is ON HOLD until Paper Publication Authors: Klima, M., Baumlova, A., Chalupska, D., Boura, E. Description: Crystal structure of the phosphatid...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the phosphatidylinositol 4-kinase IIbeta== | |
| + | <StructureSection load='4wtv' size='340' side='right'caption='[[4wtv]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wtv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WTV 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]] 1.9Å</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=4wtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wtv OCA], [https://pdbe.org/4wtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wtv RCSB], [https://www.ebi.ac.uk/pdbsum/4wtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wtv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/P4K2B_HUMAN P4K2B_HUMAN] Together with PI4K2A and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. This contribution may be especially significant in plasma membrane, endosomal and Golgi compartments. The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). Contributes to the production of InsP3 in stimulated cells and is likely to be involved in the regulation of vesicular trafficking.<ref>PMID:11923287</ref> [https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 IIbeta and PI4K IIalpha. In this study, two crystal structures are presented: the structure of human PI4K IIbeta and the structure of PI4K IIalpha containing a nucleoside analogue. The former, a complex with ATP, is the first high-resolution (1.9 A) 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. | ||
| - | + | The high-resolution crystal structure of phosphatidylinositol 4-kinase IIbeta and the crystal structure of phosphatidylinositol 4-kinase IIalpha containing a nucleoside analogue provide a structural basis for isoform-specific inhibitor design.,Klima M, Baumlova A, Chalupska D, Hrebabecky H, Dejmek M, Nencka R, Boura E Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1555-63. doi:, 10.1107/S1399004715009505. Epub 2015 Jun 30. PMID:26143926<ref>PMID:26143926</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4wtv" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Phosphatidylinositol 4-kinase|Phosphatidylinositol 4-kinase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Baumlova A]] | ||
| + | [[Category: Boura E]] | ||
| + | [[Category: Chalupska D]] | ||
| + | [[Category: Klima M]] | ||
Current revision
Crystal structure of the phosphatidylinositol 4-kinase IIbeta
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