The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured (Articolo in rivista)

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  • The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1110/ps.062115406 (literal)
Alternative label
  • Nardini M.; Svergun D.; Konarev P.V.;, Spano S.; Fasano M.; Bracco C.; Pesce A.; Donadini A.; Cericola C.; Secundo F.; Luini A.; Corda D.; Bolognesi M. (2006)
    The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured
    in Protein science (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Nardini M.; Svergun D.; Konarev P.V.;, Spano S.; Fasano M.; Bracco C.; Pesce A.; Donadini A.; Cericola C.; Secundo F.; Luini A.; Corda D.; Bolognesi M. (literal)
Pagina inizio
  • 1042 (literal)
Pagina fine
  • 1050 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 15 (literal)
Rivista
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  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Milan, Dept Biomol Sci & Biotechnol, I-20131 Milan, Italy; Univ Milan, INFM, CNR, I-20131 Milan, Italy; European Mol Biol Lab, Hamburg Outstn, D-22603 Hamburg, Germany; Russian Acad Sci, Inst Crystallog, Moscow 117333, Russia; Consorzio Mario Negri Sud, Dept Cell Biol & Oncol, I-66030 Santa Maria Imbaro, Italy; Univ Insubria, Dept Funct & Struct Biol, I-21052 Busto Arsizio, Varese, Italy; Univ Insubria, Ctr Neurosci, I-21052 Busto Arsizio, Varese, Italy; Bioind Pk Canavese, I-10010 Turin, Italy; Univ Genoa, CNR, INFM, Dept Phys, I-16146 Genoa, Italy; Univ Genoa, Ctr Excellence Biomed Res, I-16146 Genoa, Italy; CNR, Ist Chim Riconoscimento Mol, I-20131 Milan, Italy (literal)
Titolo
  • The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured (literal)
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 (similar to 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. (literal)
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