Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding and dimerization.,Nardini M, Valente C, Ricagno S, Luini A, Corda D, Bolognesi M Biochem Biophys Res Commun. 2009 Mar 27;381(1):70-4. Epub 2009 Feb 10. PMID:19351597[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nardini M, Valente C, Ricagno S, Luini A, Corda D, Bolognesi M. CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding and dimerization. Biochem Biophys Res Commun. 2009 Mar 27;381(1):70-4. Epub 2009 Feb 10. PMID:19351597 doi:10.1016/j.bbrc.2009.02.010
