ArticleBiochimica et biophysica acta2010
A cancer-derived mutation in the PSTAIRE helix of cyclin-dependent kinase 2 alters the stability of cyclin binding.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- The role of cyclin Y in normal and pathological cells.Cell cycle (Georgetown, Tex.) · 2023Review
- Inhibition mechanism of CDK-2 and GSK-3β by a sulfamoylphenyl derivative of indoline-a molecular dynamics study.Journal of molecular modeling · 2017Article
- Polygenic in vivo validation of cancer mutations using transposons.Genome biology · 2014Article
- Overexpression of DOC-1R inhibits cell cycle G1/S transition by repressing CDK2 expression and activation.International journal of biological sciences · 2013Article
- Insights into the phosphoryl transfer mechanism of cyclin-dependent protein kinases from ab initio QM/MM free-energy studies.The journal of physical chemistry. B · 2011Article
- Transferable scoring function based on semiempirical quantum mechanical PM6-DH2 method: CDK2 with 15 structurally diverse inhibitors.Journal of computer-aided molecular design · 2011Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Cyclin-dependent kinase 2 (cdk2) is a central regulator of the mammalian cell cycle. Here we describe the properties of a mutant form of cdk2 identified during large-scale sequencing of protein kinases from cancerous tissue. The mutation substituted a leucine for a proline in the PSTAIRE helix, the central motif in the interaction of the cdk with its regulatory cyclin subunit. We demonstrate that whilst the mutant cdk2 is considerably impaired in stable cyclin association, it is still able to generate an active kinase that can functionally complement defective cdks in vivo. Molecular dynamic simulations and biophysical measurements indicate that the observed biochemical properties likely stem from increased flexibility within the cyclin-binding helix.
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Registered trials
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