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TitleStructure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode
Journal, issue, pagesJ. Biol. Chem., Vol. 283, Page 27165-27178, Year 2008
Publish dateMay 28, 2004 (structure data deposition date)
AuthorsLi, H. / Koshiba, S. / Hayashi, F. / Tochio, N. / Tomizawa, T. / Kasai, T. / Yabuki, T. / Motoda, Y. / Harada, T. / Watanabe, S. ...Li, H. / Koshiba, S. / Hayashi, F. / Tochio, N. / Tomizawa, T. / Kasai, T. / Yabuki, T. / Motoda, Y. / Harada, T. / Watanabe, S. / Inoue, M. / Hayashizaki, Y. / Tanaka, A. / Kigawa, T. / Yokoyama, S.
External linksJ. Biol. Chem. / PubMed:18650440
MethodsNMR (solution)
Structure data

PDB-1wgu:
Solution Structure of the C-terminal Phosphotyrosine Interaction Domain of APBB2 from Mouse
Method: SOLUTION NMR

PDB-2roz:
Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode
Method: SOLUTION NMR

PDB-2ysz:
Solution structure of the chimera of the C-terminal PID domain of Fe65L and the C-terminal tail peptide of APP
Method: SOLUTION NMR

PDB-2yt0:
Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
Method: SOLUTION NMR

PDB-2yt1:
Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
Method: SOLUTION NMR

Source
  • mus musculus (house mouse)
KeywordsPROTEIN BINDING / phosphotyrosine-interaction domain / amyloid disease / structural genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI / PEPTIDE BINDING PROTEIN / Fe65L1 / PID domain / amyloid precursor protein / Alternative splicing / Amyloid / Apoptosis / Cell adhesion / Coated pit / Copper / Endocytosis / Glycoprotein / Heparin-binding / Iron / Membrane / Metal-binding / Notch signaling pathway / Phosphoprotein / Protease inhibitor / Serine protease inhibitor / Transmembrane / Zinc / NPPSFA / National Project on Protein Structural and Functional Analyses / Chimera / Fe65L

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