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1 Department of Biomolecular Sciences and Biotechnology, and CNR-INFM, University of Milano, I-20131 Milano, Italy
2 European Molecular Biology Laboratory, Hamburg Outstation, 22603 Hamburg, Germany
3 Institute of Crystallography, Russian Academy of Sciences, 117333 Moscow, Russia
4 Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, I-66030 Santa Maria Imbaro (Chieti), Italy
5 Department of Functional and Structural Biology, and Center of Neurosciences, University of Insubria, I-21052 Busto Arsizio (Varese), Italy
6 Bioindustry Park Canavese, I-10010 Colleretto Giacosa (Torino), Italy
7 Department of Physics, CNR-INFM and Center for Excellence in Biomedical Research, University of Genova, I-16146 Genova, Italy
8 Istituto di Chimica del Riconoscimento Molecolare, CNR, I-20131, Milano, Italy
(RECEIVED January 26, 2006; FINAL REVISION January 26, 2006; ACCEPTED January 31, 2006)
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 (
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.
Keywords: CtBP; circular dichroism; SAXS; protein-NMR; intrinsically disordered proteins; transcription corepressor
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