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-Structure paper
Title | Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode |
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Journal, issue, pages | J. Biol. Chem., Vol. 283, Page 27165-27178, Year 2008 |
Publish date | May 28, 2004 (structure data deposition date) |
Authors | Li, 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 links | J. Biol. Chem. / PubMed:18650440 |
Methods | NMR (solution) |
Structure data | PDB-1wgu: PDB-2roz: PDB-2ysz: PDB-2yt0: PDB-2yt1: |
Source |
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Keywords | PROTEIN 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 |