Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain.

Shaw, Alison Z; Martin-Malpartida, Pau; Morales, Begoña; Yraola, Francesc; Royo, Miriam; Macias, Maria J

Shaw, Alison Z; Martin-Malpartida, Pau; Morales, Begoña; Yraola, Francesc; Royo, Miriam; Macias, Maria J.

Affiliation

Shaw AZ; ICREA and the Biomedical Research Institute of Barcelona, Barcelona Science Park, Barcelona, Spain.

Proteins ; 60(3): 558-60, 2005 Aug 15.

Article in En | MEDLINE | ID: mdl-15971201

Subject(s)

Biophysics/methods; Proteomics/methods; Serine/chemistry; Threonine/chemistry; Ubiquitin-Protein Ligases/chemistry; Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites; Magnetic Resonance Spectroscopy; Mice; Molecular Sequence Data; Phosphorylation; Protein Binding; Protein Folding; Protein Structure, Tertiary

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Collection: 01-internacional Database: MEDLINE Main subject: Serine / Threonine / Biophysics / Proteomics / Ubiquitin-Protein Ligases Limits: Animals Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 2005 Document type: Article Affiliation country: Spain

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