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2ROZ

Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode

Summary for 2ROZ
Entry DOI10.2210/pdb2roz/pdb
NMR InformationBMRB: 10236
Descriptorpeptide from Amyloid beta A4 protein, Amyloid beta A4 precursor protein-binding family B member 2 (2 entities in total)
Functional Keywordsfe65l1, 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, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, peptide binding protein
Biological sourceMus musculus (mouse)
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Cellular locationMembrane; Single-pass type I membrane protein: P12023
Total number of polymer chains2
Total formula weight18586.73
Authors
Li, H.,Koshiba, S.,Tochio, N.,Watanabe, S.,Harada, T.,Inoue, M.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2008-04-25, release date: 2008-07-22, Last modification date: 2022-03-16)
Primary citationLi, 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: 18650440
DOI: 10.1074/jbc.M803892200
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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