Cyclin-dependent kinase inhibition: an opportunity to target protein-protein interactions

Research output: Chapter in Book/Report/Conference proceedingChapter

8 Scopus citations


Cyclin-dependent kinases (CDKs) play an integral part in cellular activities. To date, most of the activities have been evaluated in the cell cycle and transcription. Several diseases are affected by abnormalities in CDKs, related-pathways, or proteins that regulate CDK activity. CDKs are primarily dependent on activation by binding other proteins, namely Cyclins. In addition, phosphorylation of key CDK residues also plays a major part in CDK activity. To date, the most successful drugs have been developed against CDK4 and CDK6 and are FDA approved for use in advanced breast cancer. However, this is likely only a small fraction of the potential for targeting CDKs as a strategy against cancer and other diseases. Based on the extensive protein-protein interactions made by CDKs with other proteins (Cyclins and others), there are numerous possibilities for targeting strategies against protein-protein interactions. Here we describe the predominant roles of CDKs in the cell, key interacting proteins, significant 3-dimensional structural characteristics, and summarize the work-to-date in inhibition of CDKs.

Original languageEnglish (US)
Title of host publicationAdvances in Protein Chemistry and Structural Biology
EditorsRossen Donev
PublisherAcademic Press Inc.
Number of pages27
ISBN (Print)9780128168462
StatePublished - 2020

Publication series

NameAdvances in Protein Chemistry and Structural Biology
ISSN (Print)1876-1623
ISSN (Electronic)1876-1631

Bibliographical note

Funding Information:
Research Support: This work was supported by a grant from the Department of Defense (CA120102, M.A.K.)

Publisher Copyright:
© 2020 Elsevier Inc.


  • Cell cycle
  • Cyclin
  • Cyclin-dependent kinase
  • Protein-protein interactions
  • Structural biology
  • Transcription

PubMed: MeSH publication types

  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Review


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