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2yt1
From Proteopedia
| 2yt1, 20 NMR models () | |||||||||
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| Domains: | Fe65_C | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
Fe65L1, a member of the Fe65 family, is an adaptor protein that interacts with the cytoplasmic domain of Alzheimer amyloid precursor protein (APP) through its C-terminal phosphotyrosine interaction/phosphotyrosine binding (PID/PTB) domain. In the present study, the solution structures of the C-terminal PID domain of mouse Fe65L1, alone and in complex with a 32-mer peptide (DAAVTPEERHLSKMQQNGYENPTYKFFEQMQN) derived from the cytoplasmic domain of APP, were determined using NMR spectroscopy. The C-terminal PID domain of Fe65L1 alone exhibits a canonical PID/PTB fold, whereas the complex structure reveals a novel mode of peptide binding. In the complex structure, the NPTY motif forms a type-I beta-turn, and the residues immediately N-terminal to the NPTY motif form an antiparallel beta-sheet with the beta5 strand of the PID domain, the binding mode typically observed in the PID/PTB.peptide complex. On the other hand, the N-terminal region of the peptide forms a 2.5-turn alpha-helix and interacts extensively with the C-terminal alpha-helix and the peripheral regions of the PID domain, representing a novel mode of peptide binding that has not been reported previously for the PID/PTB.peptide complex. The indispensability of the N-terminal region of the peptide for the high affinity of the PID-peptide interaction is consistent with NMR titration and isothermal calorimetry data. The extensive binding features of the PID domain of Fe65L1 with the cytoplasmic domain of APP provide a framework for further understanding of the function, trafficking, and processing of APP modulated by adapter proteins.
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., 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, J Biol Chem. 2008 Oct 3;283(40):27165-78. Epub 2008 Jul 23. PMID:18650440
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2YT1 is a 1 chain structure of sequence from Mus musculus. Full experimental information is available from OCA.
Reference
- 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. 2008 Oct 3;283(40):27165-78. Epub 2008 Jul 23. PMID:18650440
Page seeded by OCA on Tue Feb 17 07:10:39 2009
Categories: Mus musculus | Harada, T. | Kigawa, T. | Koshiba, S. | Li, H. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Watanabe, S. | Yokoyama, S. | Amyloid precursor protein | Chimera | Fe65l | National project on protein structural and functional analyse | Nppsfa | Pid domain | Protein binding | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
