Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein

PLoS One. 2013 Jun 14;8(6):e65605. doi: 10.1371/journal.pone.0065605. Print 2013.


AIDA1 links persistent chemical signaling events occurring at the neuronal synapse with global changes in gene expression. Consistent with its role as a scaffolding protein, AIDA1 is composed of several protein-protein interaction domains. Here we report the NMR structure of the carboxy terminally located phosphotyrosine binding domain (PTB) that is common to all AIDA1 splice variants. A comprehensive survey of peptides identified a consensus sequence around an NxxY motif that is shared by a number of related neuronal signaling proteins. Using peptide arrays and fluorescence based assays, we determined that the AIDA1 PTB domain binds amyloid protein precursor (APP) in a similar manner to the X11/Mint PTB domain, albeit at reduced affinity (∼10 µM) that may allow AIDA1 to effectively sample APP, as well as other protein partners in a variety of cellular contexts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid beta-Protein Precursor / chemistry*
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Circular Dichroism
  • Conserved Sequence
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Intracellular Signaling Peptides and Proteins
  • Ligands
  • Molecular Docking Simulation
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / chemistry*
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Solubility
  • Structural Homology, Protein


  • ANKS1B protein, human
  • Amyloid beta-Protein Precursor
  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • Ligands
  • Peptide Fragments