TY - JOUR
T1 - The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured
AU - Nardini, Marco
AU - Svergun, Dmitri
AU - Konarev, Peter V.
AU - Spanò, Stefania
AU - Fasano, Mauro
AU - Bracco, Chiara
AU - Pesce, Alessandra
AU - Donadini, Alessandra
AU - Cericola, Claudia
AU - Secundo, Francesco
AU - Luini, Alberto
AU - Corda, Daniela
AU - Bolognesi, Martino
PY - 2006/5
Y1 - 2006/5
N2 - 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. Published by Cold Spring Harbor Laboratory Press.
AB - 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. Published by Cold Spring Harbor Laboratory Press.
KW - Circular dichroism
KW - CtBP
KW - Intrinsically disordered proteins
KW - Protein-NMR
KW - SAXS
KW - Transcription corepressor
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U2 - 10.1110/ps.062115406
DO - 10.1110/ps.062115406
M3 - Article
C2 - 16597837
AN - SCOPUS:33646156874
VL - 15
SP - 1042
EP - 1050
JO - Protein Science
JF - Protein Science
SN - 0961-8368
IS - 5
ER -