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The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction.
Ramos, Andres; Hollingworth, David; Adinolfi, Salvatore; Castets, Marie; Kelly, Geoff; Frenkiel, Thomas A; Bardoni, Barbara; Pastore, Annalisa.
Afiliação
  • Ramos A; Molecular Structure Division, National Institute for Medical Research, London NW7 1AA, UK.
Structure ; 14(1): 21-31, 2006 Jan.
Article em En | MEDLINE | ID: mdl-16407062
ABSTRACT
FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a modular RNA binding protein thought to be involved in posttranslational regulation. We have solved the structure in solution of the N-terminal domain of FMRP (NDF), a functionally important region involved in multiple interactions. The structure consists of a composite fold comprising two repeats of a Tudor motif followed by a short alpha helix. The interactions between the three structural elements are essential for the stability of the NDF fold. Although structurally similar, the two repeats have different dynamic and functional properties. The second, more flexible repeat is responsible for interacting both with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF contains a 3D nucleolar localization signal, since destabilization of its fold leads to altered nucleolar localization of FMRP. We suggest that the NDF composite fold determines an allosteric mechanism that regulates the FMRP functions.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Mapeamento de Interação de Proteínas / Proteína do X Frágil da Deficiência Intelectual Limite: Humans Idioma: En Ano de publicação: 2006 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Mapeamento de Interação de Proteínas / Proteína do X Frágil da Deficiência Intelectual Limite: Humans Idioma: En Ano de publicação: 2006 Tipo de documento: Article