Solution Structure of the C-terminal Phosphotyrosine Interaction Domain of APBB2 from Mouse

Summary for 1WGU

Descriptoramyloid beta (A4) precursor protein-binding, family B, member 2 (1 entity in total)
Functional Keywordsphosphotyrosine-interaction domain, amyloid disease, structural genomics, riken structural genomics/proteomics initiative, rsgi, protein binding
Biological sourceMus musculus (house mouse)
Total number of polymer chains1
Total molecular weight14750.55
Li, H.,Hayashi, F.,Koshiba, S.,Inoue, M.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-28, release date: 2004-11-28, Last modification date: 2011-07-13)
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
PubMed: 18650440 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M803892200
MImport into Mendeley
Experimental method
NMR Information

Structure validation

ClashscoreRamachandran outliersSidechain outliers211.2%17.4%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures