4md9
From Proteopedia
(Difference between revisions)
(3 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
+ | |||
==Crystal Structure of symmetric CK2 holoenzyme with mutated alpha subunit (F121E truncated at aa 336)== | ==Crystal Structure of symmetric CK2 holoenzyme with mutated alpha subunit (F121E truncated at aa 336)== | ||
- | <StructureSection load='4md9' size='340' side='right' caption='[[4md9]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='4md9' size='340' side='right'caption='[[4md9]], [[Resolution|resolution]] 3.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4md9]] is a 16 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4md9]] is a 16 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=4MD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MD9 FirstGlance]. <br> |
- | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
- | <tr><td class="sblockLbl"><b>[[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4md9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4md9 OCA], [https://pdbe.org/4md9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4md9 RCSB], [https://www.ebi.ac.uk/pdbsum/4md9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4md9 ProSAT]</span></td></tr> |
- | + | </table> | |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | == Function == |
- | <table> | + | [https://www.uniprot.org/uniprot/CSK2B_HUMAN CSK2B_HUMAN] Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit.<ref>PMID:11239457</ref> <ref>PMID:16818610</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 15: | Line 16: | ||
Active Form of the Protein Kinase CK2 alphabeta Holoenzyme Is a Strong Complex with Symmetric Architecture.,Lolli G, Ranchio A, Battistutta R ACS Chem Biol. 2013 Nov 11. PMID:24175891<ref>PMID:24175891</ref> | Active Form of the Protein Kinase CK2 alphabeta Holoenzyme Is a Strong Complex with Symmetric Architecture.,Lolli G, Ranchio A, Battistutta R ACS Chem Biol. 2013 Nov 11. PMID:24175891<ref>PMID:24175891</ref> | ||
- | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
+ | <div class="pdbe-citations 4md9" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Casein kinase 3D structures|Casein kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Battistutta | + | [[Category: Battistutta R]] |
- | [[Category: Lolli | + | [[Category: Lolli G]] |
- | [[Category: Ranchio | + | [[Category: Ranchio A]] |
- | + | ||
- | + |
Current revision
Crystal Structure of symmetric CK2 holoenzyme with mutated alpha subunit (F121E truncated at aa 336)
|