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Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7.

Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7. Research Abstract Details 

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  • Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7. Abstract Text:

    laura tornatoreLaura Tornatore,daniela marascoDaniela Marasco,nina dathanNina Dathan,rosa maria vitaleRosa Maria Vitale,ettore benedettiEttore Benedetti,salvatore papaSalvatore Papa,guido franzosoGuido Franzoso,menotti ruvoMenotti Ruvo,simona maria montiSimona Maria Monti,laura tornatoreLaura Tornatore,daniela marascoDaniela Marasco,nina dathanNina Dathan,rosa maria vitaleRosa Maria Vitale,ettore benedettiEttore Benedetti,salvatore papaSalvatore Papa,guido franzosoGuido Franzoso,menotti ruvoMenotti Ruvo,simona maria montiSimona Maria Monti,

    Gadd45alpha, 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, Gadd45beta has been indicated as a major player in the endogenous NF-kappaB-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 Gadd45beta-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 Gadd45beta 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 Gadd45alpha. 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.

    Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7. Publishing Authors By Initials

    l tornatoreL Tornatore,d marascoD Marasco,n dathanN Dathan,rm vitaleRM Vitale,e benedettiE Benedetti,s papaS Papa,g franzosoG Franzoso,m ruvoM Ruvo,sm montiSM Monti,l tornatoreL Tornatore,d marascoD Marasco,n dathanN Dathan,rm vitaleRM Vitale,e benedettiE Benedetti,s papaS Papa,g franzosoG Franzoso,m ruvoM Ruvo,sm montiSM Monti,

    For similar abstracts research abstracts see: abstracts research

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    Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of molecular biology

    VOLUME: 378

    Page Numbers: 97-111

    Journal Abbreviation:

    ISSN: 1089-8638

    DAY: 4

    MONTH: 02

    YEAR: 2008

    Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985088

    Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7. Keywords Mesh Terms:

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    Grant and Affiliation Information for Gadd45beta forms a Homodimeric Complex that Binds Tightly to MKK7.

    AFFILIATION: Istituto di Biostrutture e Bioimmagini (IBB), CNR, via Mezzocannone, 16, 80134, Napoli, Italy; Dipartimento delle Scienze Biologiche, via Mezzocannone, 16, 80134, Napoli, Italy.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: J Mol Biol

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