ArticleStructure (London, England : 1993)2022
Crystal structure of the CDK11 kinase domain bound to the small-molecule inhibitor OTS964.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Cyclins and Cyclin-Dependent Kinases: Structure, Biological Functions, and Innovative Targeting Strategies in Cancer.MedComm · 2026Review
- Targeting CDKs in the RNAPII transcription cycle.Nature reviews. Drug discovery · 2026Review
- SF3B1 phosphorylation is an evolutionarily conserved step in spliceosome activation carried out by the divergent, OTS964-insensitive kinase CRK9 in trypanosomes.Nucleic acids research · 2026Article
- Cryo-EM structures of the CDK11-cyclin L-SAP30BP complex reveal mechanisms of CDK11 regulation.Nature communications · 2026Article
- An AKR1C3-activated kinase inhibitor prodrug.RSC chemical biology · 2026Article
- Targeting CDK11 in Rhabdoid Tumor of the Kidney.Cancers · 2026Article
- Targeting cyclin-dependent kinase 11: a computational approach for natural anti-cancer compound discovery.Molecular diversity · 2025Article
- Targeting Transcriptional Cyclin-Dependent Kinases in Cancer.Molecular cancer therapeutics · 2025Review
- Mechanistic Roles of Transcriptional Cyclin-Dependent Kinases in Oncogenesis: Implications for Cancer Therapy.Cancers · 2025Review
- Inferring Drug-Gene Relationships in Cancer Using Literature-Augmented Large Language Models.Cancer research communications · 2025Article
- CDK11 requires a critical activator SAP30BP to regulate pre-mRNA splicing.The EMBO journal · 2023Article
- Transcriptomic and genomic identification of spliceosomal genes fromActa biochimica et biophysica Sinica · 2023Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
CDK11 is a cyclin-dependent kinase that controls proliferation by regulating transcription, RNA splicing, and the cell cycle. As its activity is increasingly associated with cancer, CDK11 is an attractive target for the development of small-molecule inhibitors. However, the development of CDK11 inhibitors with limited off-target effects against other CDKs poses a challenge based on the high conservation of sequence across family members. OTS964 is notable as it displays a measure of specificity for CDK11 in cells. To understand the basis for OTS964's specificity for CDK11, we solved a 2.6 Å crystal structure of the CDK11 kinase domain bound to OTS964. Despite the absence of cyclin, CDK11 adopts an active-like conformation when bound to OTS964. We identified amino acids likely to contribute to the specificity of OTS964 for CDK11 and assessed their contribution to OTS964 binding by isothermal titration calorimetry (ITC) in vitro and by resistance to OTS964 in cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.