1qb3

<table><tr><td colspan='2'>[[1qb3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QB3 FirstGlance]. <br>

</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=1qb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qb3 OCA], [https://pdbe.org/1qb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qb3 RCSB], [https://www.ebi.ac.uk/pdbsum/1qb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qb3 ProSAT]</span></td></tr>

[[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.

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== Publication Abstract from PubMed ==

BACKGROUND: The Saccharomyces cerevisiae protein Cks1 (cyclin-dependent kinase subunit 1) is essential for cell-cycle progression. The biological function of Cks1 can be modulated by a switch between two distinct molecular assemblies: the single domain fold, which results from the closing of a beta-hinge motif, and the intersubunit beta-strand interchanged dimer, which arises from the opening of the beta-hinge motif. The crystal structure of a cyclin-dependent kinase (Cdk) in complex with the human Cks homolog CksHs1 single-domain fold revealed the importance of conserved hydrophobic residues and charged residues within the beta-hinge motif. RESULTS: The 3.0 A resolution Cks1 structure reveals the strict structural conservation of the Cks alpha/beta-core fold and the beta-hinge motif. The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure. This Cks1 structure confirms the conservation of the Cks anion-binding site, which interacts with sidechain residues from the C-terminal alpha helix of another subunit in the crystal. CONCLUSIONS: The Cks1 structure exemplifies the conservation of the beta-interchanged dimer and the anion-binding site in evolutionarily distant yeast and human Cks homologs. Mutational analyses including in vivo rescue of CKS1 disruption support the dual functional roles of the beta-hinge residue Glu94, which participates in Cdk binding, and of the anion-binding pocket that is located 22 A away and on an opposite face to Glu94. The Cks1 structure suggests a biological role for the beta-interchanged dimer and the anion-binding site in targeting Cdks to specific phosphoproteins during cell-cycle progression.

Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions.,Bourne Y, Watson MH, Arvai AS, Bernstein SL, Reed SI, Tainer JA Structure. 2000 Aug 15;8(8):841-50. PMID:10997903<ref>PMID:10997903</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Arvai, A S]]

[[Category: Bernstein, S L]]

[[Category: Bourne, Y]]

[[Category: Reed, S I]]

[[Category: Tainer, J A]]

[[Category: Watson, M H]]

[[Category: Cyclin-dependent kinase]]