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The crystal structure of a major dust mite allergen Der p 2, and its biological implications.
Derewenda, U; Li, J; Derewenda, Z; Dauter, Z; Mueller, G A; Rule, G S; Benjamin, D C.
Afiliación
  • Derewenda U; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA. ud3a@virginia.edu
J Mol Biol ; 318(1): 189-97, 2002 Apr 19.
Article en En | MEDLINE | ID: mdl-12054778
The crystal structure of the common house mite (Dermatophagoides sp.) Der p 2 allergen was solved at 2.15 A resolution using the MAD phasing technique, and refined to an R-factor of 0.209. The refined atomic model, which reveals an immunoglobulin-like tertiary fold, differs in important ways from the previously described NMR structure, because the two beta-sheets are significantly further apart and create an internal cavity, which is occupied by a hydrophobic ligand. This interaction is structurally reminiscent of the binding of a prenyl group by a regulatory protein, the Rho guanine nucleotide exchange inhibitor. The crystal structure suggests that binding of non-polar molecules may be essential to the physiological function of the Der p 2 protein.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Mol Biol Año: 2002 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Buscar en Google
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PubMed Links

Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Mol Biol Año: 2002 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos