1. The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured.
- Author
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Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, and Bolognesi M
- Subjects
- Alcohol Oxidoreductases, Amino Acid Sequence, Binding Sites, Circular Dichroism, DNA-Binding Proteins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Phosphoproteins, Protein Folding, Repressor Proteins chemistry, Transcription Factors chemistry, Transcription, Genetic
- Abstract
C-terminal binding proteins (CtBPs) are moonlighting proteins involved in nuclear transcriptional corepression and in Golgi membrane tubule fission. Structural information on CtBPs is available for their substrate-binding domain, responsible for transcriptional repressor recognition/binding, and for the nucleotide-binding domain, involved in NAD(H)-binding and dimerization. On the contrary, little is known about the structure of CtBP C-terminal region ( approximately 90 residues), hosting sites for post-translational modifications. In the present communication we apply a combined approach based on bioinformatics, nuclear magnetic resonance, circular dichroism spectroscopy, and small-angle X-ray scattering, and we show that the CtBP C-terminal region is intrinsically unstructured in the full-length CtBP and in constructs lacking the substrate- and/or the nucleotide-binding domains. The flexible nature of this protein region, and its structural transitions, may be instrumental for CtBP recognition and binding to diverse molecular partners.
- Published
- 2006
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