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Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain.
Zhou, M M; Huang, B; Olejniczak, E T; Meadows, R P; Shuker, S B; Miyazaki, M; Trüb, T; Shoelson, S E; Fesik, S W.
Afiliación
  • Zhou MM; Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA.
Nat Struct Biol ; 3(4): 388-93, 1996 Apr.
Article en En | MEDLINE | ID: mdl-8599766
We present the NMR structure of the PTB domain of insulin receptor substrate-1 (IRS-1) complexed to a tyrosine-phosphorylated peptide derived from the IL-4 receptor. Despite the lack of sequence homology and different binding specificity, the overall fold of the protein is similar to that of the Shc PTB domain and closely resembles that of PH domains. However, the PTB domain of IRS-1 is smaller than that of Shc (110 versus 170 residues) and binds to phosphopeptides in a distinct manner. We explain the phosphopeptide binding specificity based on the structure of the complex and results of site-directed mutagenesis experiments.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfopéptidos / Fosfoproteínas / Antígenos CD / Receptores de Interleucina Tipo de estudio: Prognostic_studies Idioma: En Revista: Nat Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1996 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfopéptidos / Fosfoproteínas / Antígenos CD / Receptores de Interleucina Tipo de estudio: Prognostic_studies Idioma: En Revista: Nat Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1996 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos