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TitleCryo-EM structure of the CDK2-cyclin A-CDC25A complex.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 6807, Year 2024
Publish dateAug 9, 2024
AuthorsRhianna J Rowland / Svitlana Korolchuk / Marco Salamina / Natalie J Tatum / James R Ault / Sam Hart / Johan P Turkenburg / James N Blaza / Martin E M Noble / Jane A Endicott /
PubMed AbstractThe cell division cycle 25 phosphatases CDC25A, B and C regulate cell cycle transitions by dephosphorylating residues in the conserved glycine-rich loop of CDKs to activate their activity. Here, we ...The cell division cycle 25 phosphatases CDC25A, B and C regulate cell cycle transitions by dephosphorylating residues in the conserved glycine-rich loop of CDKs to activate their activity. Here, we present the cryo-EM structure of CDK2-cyclin A in complex with CDC25A at 2.7 Å resolution, providing a detailed structural analysis of the overall complex architecture and key protein-protein interactions that underpin this 86 kDa complex. We further identify a CDC25A C-terminal helix that is critical for complex formation. Sequence conservation analysis suggests CDK1/2-cyclin A, CDK1-cyclin B and CDK2/3-cyclin E are suitable binding partners for CDC25A, whilst CDK4/6-cyclin D complexes appear unlikely substrates. A comparative structural analysis of CDK-containing complexes also confirms the functional importance of the conserved CDK1/2 GDSEID motif. This structure improves our understanding of the roles of CDC25 phosphatases in CDK regulation and may inform the development of CDC25-targeting anticancer strategies.
External linksNat Commun / PubMed:39122719 / PubMed Central
MethodsEM (single particle)
Resolution2.7 Å
Structure data

19408

8roz

EMDB-19408, PDB-8roz:
Cryo-EM structure of CDK2-cyclin A in complex with CDC25A
Method: EM (single particle) / Resolution: 2.7 Å

Source
  • homo sapiens (human)
  • bos taurus (domestic cattle)
KeywordsCELL CYCLE / cell-cycle / CDK / phosphatase / cancer

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