3qy2

<StructureSection load='3qy2' size='340' side='right' caption='[[3qy2]], [[Resolution|resolution]] 2.59&Aring;' scene=''>

<table><tr><td colspan='2'>[[3qy2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QY2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QY2 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene><br>

<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CKS1, YBR135W, YBR1011 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qy2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qy2 RCSB], [http://www.ebi.ac.uk/pdbsum/3qy2 PDBsum]</span></td></tr>

<table>

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== Publication Abstract from PubMed ==

Cks (cyclin-dependent kinase subunit) proteins are essential eukaryotic cell cycle regulatory proteins that physically associate with cyclin-dependent kinases (Cdks) to modulate their activity. Cks proteins have also been studied for their ability to form domain-swapped dimers by exchanging beta-strands. Domain swapping is mediated by a conserved beta-hinge region containing two proline residues. Previous structural studies indicate that Cks in its dimer form is unable to bind Cdk, suggesting that the monomer-dimer equilibrium of Cks may have an effect on Cks-mediated Cdk regulation. We present the crystal structure of a proline-to-alanine mutant Saccharomyces cerevisiae Cks protein (Cks1 P93A) that preferentially adopts the monomer conformation but surprisingly fails to bind Cdk. Comparison of the Cks1 P93A structure to that of other Cks proteins reveals that Pro93 is critical for stabilizing a multiple beta-turn structure in the hinge region that properly positions an essential Cdk-binding residue. Additionally, we find that these beta-turn formations, conserved in Cks homologs, have implications for the mechanism and preferentiality of strand exchange. Together, our observations suggest that the conservation of Cks hinge-region prolines reflects their functions in forming a Cdk binding interface and that the ability of these prolines to control partitioning between monomer and dimer is a consequence of the beta-turn networks within the hinge.

 

== References ==

[[Category: Balog, E R.M.]]

[[Category: Finch, W.]]

[[Category: Harvey, S L.]]

[[Category: Hoeft, C O.]]

[[Category: Kellogg, D K.]]

[[Category: Rubin, S M.]]

[[Category: Saetern, O C.]]

[[Category: Thai, V.]]

[[Category: Ubiquitin binding]]