Simulations of a specific inhibitor of the dishevelled PDZ domain

Xin Chen, Yuefan Deng

Research output: Contribution to journalArticlepeer-review


The dishevelled (Dvl) PDZ domain is believed to play an essential role in the canonical and noncanonical Wnt signaling pathways, which are involved in embryo development as well as in tumorigenesis. Also, it binds directly to frizzled (Fz) receptors. An organic molecule (NSC668036) from the National Cancer Institute small-molecule library has been identified to be able to bind to the Dvl PDZ domain. Molecular dynamics simulation was used to provide detailed analyses of the binding between them.

Original languageEnglish (US)
Pages (from-to)91-96
Number of pages6
JournalJournal of Molecular Modeling
Issue number1
StatePublished - 2009


  • Dishevelled PDZ domain
  • Molecular dynamics
  • Protein docking

ASJC Scopus subject areas

  • Catalysis
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry
  • Computational Theory and Mathematics


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