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

Biochem Biophys Res Commun. 2009 Mar 27;381(1):70-4. doi: 10.1016/j.bbrc.2009.02.010. Epub 2009 Feb 10.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Crystallography, X-Ray
  • Glutamic Acid / genetics
  • Glutamic Acid / metabolism*
  • Glycine / genetics
  • Glycine / metabolism*
  • Mutation
  • NAD / metabolism*
  • Protein Conformation
  • Protein Multimerization
  • Rats
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*


  • Carrier Proteins
  • Ctbp1 protein, rat
  • Transcription Factors
  • NAD
  • Glutamic Acid
  • Glycine