Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 23799029.
- Also identified by DOI 10.1371/journal.pone.0065605 and PMC identifier 3683042.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Amyloid beta-Protein Precursor
- Carrier Proteins
- Peptide Fragments