View source for 4lpa


==Crystal structure of a Cdc6 phosphopeptide in complex with Cks1==
<StructureSection load='4lpa' size='340' side='right'caption='[[4lpa]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lpa]] 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=4LPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LPA 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4lpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lpa OCA], [https://pdbe.org/4lpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lpa RCSB], [https://www.ebi.ac.uk/pdbsum/4lpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lpa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CKS1_YEAST CKS1_YEAST] Binds to the catalytic subunit of the cyclin dependent kinase (CDC28) and is essential for its biological function.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cks is an evolutionarily conserved protein that regulates cyclin-dependent kinase (CDK) activity. Clarifying the underlying mechanisms and cellular contexts of Cks function is critical because Cks is essential for proper cell growth, and its overexpression has been linked to cancer. We observe that budding-yeast Cks associates with select phosphorylated sequences in cell cycle-regulatory proteins. We characterize the molecular interactions responsible for this specificity and demonstrate that Cks enhances CDK activity in response to specific priming phosphosites. Identification of the binding consensus sequence allows us to identify putative Cks-directed CDK substrates and binding partners. We characterize new Cks-binding sites in the mitotic regulator Wee1 and discover a new role for Cks in regulating CDK activity at mitotic entry. Together, our results portray Cks as a multifunctional phosphoadaptor that serves as a specificity factor for CDK activity.

Cks confers specificity to phosphorylation-dependent CDK signaling pathways.,McGrath DA, Balog ER, Koivomagi M, Lucena R, Mai MV, Hirschi A, Kellogg DR, Loog M, Rubin SM Nat Struct Mol Biol. 2013 Dec;20(12):1407-14. doi: 10.1038/nsmb.2707. Epub 2013, Nov 3. PMID:24186063<ref>PMID:24186063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lpa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cyclin-dependent kinase regulatory subunit 3D structures|Cyclin-dependent kinase regulatory subunit 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Balog ERM]]
[[Category: Hirschi A]]
[[Category: Kellogg DR]]
[[Category: Koivomagi M]]
[[Category: Loog M]]
[[Category: Lucena R]]
[[Category: Mai MV]]
[[Category: McGrath DA]]
[[Category: Rubin SM]]