This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4yc4
From Proteopedia
(Difference between revisions)
m (Protected "4yc4" [edit=sysop:move=sysop]) |
|||
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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 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=4YC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YC4 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]] 2.58Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yc4 OCA], [https://pdbe.org/4yc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yc4 RCSB], [https://www.ebi.ac.uk/pdbsum/4yc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yc4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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.[https://www.uniprot.org/uniprot/D9IEF7_BPT4 D9IEF7_BPT4] | ||
| + | <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> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4yc4" style="background-color:#fffaf0;"></div> |
| - | [[Category: Boura | + | |
| + | ==See Also== | ||
| + | *[[Phosphatidylinositol 4-kinase|Phosphatidylinositol 4-kinase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Boura E]] | ||
| + | [[Category: Klima M]] | ||
Current revision
Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with nucleotide analog
| |||||||||||
