Gadd45 beta forms a homodimeric complex that binds tightly to MKK7 (Articolo in rivista)

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Label
  • Gadd45 beta forms a homodimeric complex that binds tightly to MKK7 (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.jmb.2008.01.074 (literal)
Alternative label
  • Tornatore L.; Marasco D.; Dathan N.; Vitale R.M.; Benedetti E.; Papa S.; Franzoso G.; Ruvo M.; Monti S.M. (2008)
    Gadd45 beta forms a homodimeric complex that binds tightly to MKK7
    in Journal of Molecular Biology; Academic Press Ltd., Elsevier Science Ltd., London (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Tornatore L.; Marasco D.; Dathan N.; Vitale R.M.; Benedetti E.; Papa S.; Franzoso G.; Ruvo M.; Monti S.M. (literal)
Pagina inizio
  • 97 (literal)
Pagina fine
  • 111 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 378 (literal)
Rivista
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  • 15 (literal)
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  • 1 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biostrutture e Bioimmagini (IBB), CNR, via Mezzocannone, 16, 80134, Napoli, Italy; Dipartimento delle Scienze Biologiche, via Mezzocannone, 16, 80134, Napoli, Italy; Istituto di Chimica Biomolecolare (ICB), CNR, Via Campi Flegrei, 34, 80078 Pozzuoli, (NA), Italy; Department of Immunology at Hammersmith, Division of Investigative Science, Imperial College, London, Du Cane Road, London W12 ONN, UK (literal)
Titolo
  • Gadd45 beta forms a homodimeric complex that binds tightly to MKK7 (literal)
Abstract
  • Gadd45 alpha, beta, and gamma proteins, also known as growth arrest and DNA damage-inducible factors, have a number of cellular functions, including cell-cycle regulation and propagation of signals produced by a variety of cellular stimuli, maintaining genomic stability and apoptosis. Furthermore, Gadd45 beta has been indicated as a major player in the endogenous NF-kB mediated resistance to apoptosis in a variety of cell lines. In fibroblasts this mechanism involves the inactivation of MKK7, the upstream activator of JNK, by direct binding within the kinase ATP pocket. On the basis of a number of experimental data, the structures of Gadd45beta and the Gadd45 beta- MKK7 complex have been predicted recently and data show that interactions are mediated by acidic loops 1 and 2, and helices 3 and 4 of Gadd45beta. Here, we provide further evidence that Gadd45 beta is a prevailingly alpha-helical protein and that in solution it is able to form non covalent dimers but not higher-order oligomers, in contrast to what has been reported for the homologous Gadd45 alpha. We show that the contact region between the two monomers is comprised of the predicted helix 1 (residues Q17-Q33) and helix 5 (residues K131-R146) of the protein, which appear to be antiparallel and to form a large dimerisation surface not involved in MKK7 recognition. The results suggest the occurrence of a large complex containing at least an MKK7-Gadd45beta:Gadd45beta-MKK7 tetrameric unit whose complexity could be further increased by the dimeric nature of the isolated MKK7. (literal)
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