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

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.

SUBMITTER: Smirnova E

PROVIDER: S-EPMC3683042 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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

Smirnova Ekaterina E Shanbhag Riya R Kurabi Arwa A Mobli Mehdi M Kwan Jamie J JJ Donaldson Logan W LW

PloS one 20130614 6

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 num ...[more]

PMID: 23799029

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