Abstract
The structural characteristics of the CtBP family of transcriptional corepressors suggest an additional role for coenzyme nicotinamide adenine dinudeotide in the repression of gene expression. Remarkably, CtBP orthologues are unique among transcriptional regulators in that they display striking primary sequence and structural similarity to the D-isomer specific 2-hydroxyacid dehydrogenase class of enzymes. Recent structural studies of rat CtBP/BARS and human CtBPl provide insight into the role of pyridine dinucleotide binding in regulation of CtBP quaternary structure, and corepression activity through association with -PXDLS-containing targets.
Keywords
- Ternary Complex
- Protein Data Bank Entry
- Transcriptional Corepressor
- Synaptic Ribbon
- Fluorescence Resonance Energy Transfer Signal
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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© 2007 Landes Bioscience and Springer Science+Business Media
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Lundblad, J.R. (2007). Structural Determinants of CtBP Function. In: GtBP Family Proteins. Molecular Biology Intelligence Unit. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39973-7_9
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DOI: https://doi.org/10.1007/978-0-387-39973-7_9
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