2YT1
Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
Summary for 2YT1
Entry DOI | 10.2210/pdb2yt1/pdb |
NMR Information | BMRB: 10239 |
Descriptor | Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2 (1 entity in total) |
Functional Keywords | chimera, fe65l, pid domain, amyloid precursor protein, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, protein binding |
Biological source | Mus musculus (mouse) |
Total number of polymer chains | 1 |
Total formula weight | 20007.11 |
Authors | Li, H.,Koshiba, S.,Watanabe, S.,Harada, T.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-04-05, release date: 2008-04-08, Last modification date: 2024-05-29) |
Primary citation | 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. 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 J.Biol.Chem., 283:27165-27178, 2008 Cited by PubMed: 18650440DOI: 10.1074/jbc.M803892200 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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