4lqq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lqq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LQQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lqq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LQQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=4lqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqq OCA], [https://pdbe.org/4lqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lqq RCSB], [https://www.ebi.ac.uk/pdbsum/4lqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqq ProSAT]</span></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=4lqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqq OCA], [https://pdbe.org/4lqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lqq RCSB], [https://www.ebi.ac.uk/pdbsum/4lqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CBK1_YEAST CBK1_YEAST] Protein kinase that seems to play a role in the regulation of cell morphogenesis and proliferation.
[https://www.uniprot.org/uniprot/CBK1_YEAST CBK1_YEAST] Protein kinase that seems to play a role in the regulation of cell morphogenesis and proliferation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic cells commonly use protein kinases in signaling systems that relay information and control a wide range of processes. These enzymes have a fundamentally similar structure, but achieve functional diversity through variable regions that determine how the catalytic core is activated and recruited to phosphorylation targets. "Hippo" pathways are ancient protein kinase signaling systems that control cell proliferation and morphogenesis; the NDR/LATS family protein kinases, which associate with "Mob" coactivator proteins, are central but incompletely understood components of these pathways. Here we describe the crystal structure of budding yeast Cbk1-Mob2, to our knowledge the first of an NDR/LATS kinase-Mob complex. It shows a novel coactivator-organized activation region that may be unique to NDR/LATS kinases, in which a key regulatory motif apparently shifts from an inactive binding mode to an active one upon phosphorylation. We also provide a structural basis for a substrate docking mechanism previously unknown in AGC family kinases, and show that docking interaction provides robustness to Cbk1's regulation of its two known in vivo substrates. Co-evolution of docking motifs and phosphorylation consensus sites strongly indicates that a protein is an in vivo regulatory target of this hippo pathway, and predicts a new group of high-confidence Cbk1 substrates that function at sites of cytokinesis and cell growth. Moreover, docking peptides arise in unstructured regions of proteins that are probably already kinase substrates, suggesting a broad sequential model for adaptive acquisition of kinase docking in rapidly evolving intrinsically disordered polypeptides.
The Structure of an NDR/LATS Kinase-Mob Complex Reveals a Novel Kinase-Coactivator System and Substrate Docking Mechanism.,Gogl G, Schneider KD, Yeh BJ, Alam N, Nguyen Ba AN, Moses AM, Hetenyi C, Remenyi A, Weiss EL PLoS Biol. 2015 May 12;13(5):e1002146. doi: 10.1371/journal.pbio.1002146., eCollection 2015 May. PMID:25966461<ref>PMID:25966461</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lqq" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 15:21, 1 March 2024

Crystal structure of the Cbk1(T743E)-Mob2 kinase-coactivator complex in crystal form BCrystal structure of the Cbk1(T743E)-Mob2 kinase-coactivator complex in crystal form B

Structural highlights

4lqq is a 4 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBK1_YEAST Protein kinase that seems to play a role in the regulation of cell morphogenesis and proliferation.

See Also

4lqq, resolution 3.60Å

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