4yc4
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with nucleotide analog== |
+ | <StructureSection load='4yc4' size='340' side='right' caption='[[4yc4]], [[Resolution|resolution]] 2.58Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4yc4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YC4 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=M59:[(1S,3S,4S)-3-(6-AMINO-9H-PURIN-9-YL)BICYCLO[2.2.1]HEPT-1-YL]METHANOL'>M59</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pla|4pla]]</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yc4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yc4 RCSB], [http://www.ebi.ac.uk/pdbsum/4yc4 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/P4K2A_HUMAN P4K2A_HUMAN]] Together with PI4K2B and the type III PI4Ks (PIK4CA and PIK4CB) it contributes to the overall PI4-kinase activity of the cell. 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 (By similarity). This lipid kinase is the major phosphatidylinositol 4-phosphate (PI4P) producer in the Golgi apparatus, it generates more than 50% of this molecule which is essential for the identity of the organelle, protein sorting and membrane trafficking. | ||
+ | <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 | + | 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> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Boura, E]] | ||
[[Category: Klima, M]] | [[Category: Klima, M]] | ||
- | [[Category: | + | [[Category: Complex]] |
+ | [[Category: Inhibitor]] | ||
+ | [[Category: Kinase]] | ||
+ | [[Category: Transferase]] |
Revision as of 13:14, 15 July 2015
Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with nucleotide analog
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Categories: Boura, E | Klima, M | Complex | Inhibitor | Kinase | Transferase