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The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors.
Qian, Y Q; Billeter, M; Otting, G; Müller, M; Gehring, W J; Wüthrich, K.
Afiliación
  • Qian YQ; Institut für Molekularbiologie und Biophysik Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Cell ; 59(3): 573-80, 1989 Nov 03.
Article en En | MEDLINE | ID: mdl-2572329
ABSTRACT
The structure of the Antennapedia homeodomain from Drosophila melanogaster was determined by nuclear magnetic resonance spectroscopy in solution. It includes three well-defined helices (residues 10-21, 28-38, and 42-52) and a more flexible fourth helix (residues 53-59). Residues 30-50 form a helix-turn-helix motif virtually identical to those observed in various prokaryotic repressors. Further comparisons of the homeodomain with prokaryotic repressors showed that there are also significant differences in the molecular architectures. Overall, these studies support the view that the third helix of the homeodomain may function as the DNA recognition site. The elongation of the third helix by the fourth helix is a structured element that so far appears to be unique to the Antennapedia homeodomain.
Asunto(s)
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Base de datos: MEDLINE Asunto principal: Proteínas Represoras / Genes Homeobox / Drosophila melanogaster Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Cell Año: 1989 Tipo del documento: Article País de afiliación: Suiza
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Base de datos: MEDLINE Asunto principal: Proteínas Represoras / Genes Homeobox / Drosophila melanogaster Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Cell Año: 1989 Tipo del documento: Article País de afiliación: Suiza