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The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains.
Brockmann, Christoph; Leitner, Dietmar; Labudde, Dirk; Diehl, Annette; Sievert, Volker; Büssow, Konrad; Kühne, Ronald; Oschkinat, Hartmut.
Afiliación
  • Brockmann C; Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, D-13125 Berlin, Germany.
FEBS Lett ; 558(1-3): 101-6, 2004 Jan 30.
Article en En | MEDLINE | ID: mdl-14759524
The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358-S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas HSP70 de Choque Térmico Límite: Humans Idioma: En Revista: FEBS Lett Año: 2004 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Buscar en Google
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas HSP70 de Choque Térmico Límite: Humans Idioma: En Revista: FEBS Lett Año: 2004 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido