Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
RIKEN Structural Genomics/Proteomics Initiative (RSGI)
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
Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2
GSSGSSGDAAVTPEERHLSKMQQNGYENPTYKFFEQMQNSGPSSGIEGRGSSGSSGSSGSSGPTPKTELVQKFRVQYLGM LPVDRPVGMDTLNSAIENLMTSSSKEDWPSVNMNVADATVTVISEKNEEEVLVECRVRFLSFMGVGKDVHTFAFIMDTGN QRFECHVFWCEPNAANVSEAVQAAC
RIKEN Structural Genomics/Proteomics Initiative
NPPSFA, National Project on Protein Structural and Functional Analyses
HELIX Determination method: Author determined
SHEET Determination method: Author determined
structures with the least restraint violations, target function
1.00mM chimera sample U-15N, 13C; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O
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