CtBP1/BARS Gly172 → Glu mutant structure: Impairing NAD(H)-binding and dimerization

Marco Nardini, Carmen Valente, Stefano Ricagno, Alberto Luini, Daniela Corda, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review


C-terminal binding proteins (CtBPs) are multi-functional proteins involved in nuclear transcriptional co-repression, Golgi membrane fission, and synaptic ribbon formation. Binding of NAD(H) to CtBPs promotes dimerization. CtBP dimers act as a scaffold for multimeric protein complex formation, thus bridging transcriptional repressors and their targets in the nucleus. Based on size-exclusion chromatography experiments and on the crystal structure of the NAD(H)-free G172E CtBP mutant, we show here that absence of NAD(H) induces flexibility/backbone conformational changes at the dimerization interface and at the CtBP interdomain region. The results presented shed first light on the correlation between NAD(H)-binding and functional CtBP dimerization.

Original languageEnglish
Pages (from-to)70-74
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Mar 27 2009


  • BARS
  • CtBP
  • Dimerization
  • Golgi membrane fission
  • NAD(H)
  • Transcription co-repressor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology


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