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TitleThe C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured.
Journal, issue, pagesProtein Sci, Vol. 15, Issue 5, Page 1042-1050, Year 2006
Publish dateApr 5, 2006
AuthorsMarco Nardini / Dmitri Svergun / Peter V Konarev / Stefania Spanò / Mauro Fasano / Chiara Bracco / Alessandra Pesce / Alessandra Donadini / Claudia Cericola / Francesco Secundo / Alberto Luini / Daniela Corda / Martino Bolognesi /
PubMed AbstractC-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 ...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.
External linksProtein Sci / PubMed:16597837 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDAD4:
Full length GtBP3 (full length CtBP3, full CtBP3)
Method: SAXS/SANS

SASDAE4:
C-terminal CtBP3 (C-term part CtBP3, C-term CtBP3)
Method: SAXS/SANS

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