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

Smirnova, Ekaterina, Shanbhag, Riya, Kurabi, Arwa, Mobli, Mehdi, Kwan, Jamie J. and Donaldson, Logan W. (2013) Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein. PLoS ONE, 8 6: e65605.1-e65605.8. doi:10.1371/journal.pone.0065605

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Author Smirnova, Ekaterina
Shanbhag, Riya
Kurabi, Arwa
Mobli, Mehdi
Kwan, Jamie J.
Donaldson, Logan W.
Title Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein
Journal name PLoS ONE   Check publisher's open access policy
ISSN 1932-6203
Publication date 2013-06
Sub-type Article (original research)
DOI 10.1371/journal.pone.0065605
Open Access Status DOI
Volume 8
Issue 6
Start page e65605.1
End page e65605.8
Total pages 8
Place of publication San Francisco, CA, United States
Publisher Public Library of Science
Collection year 2014
Language eng
Formatted 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.
Keyword Amyloid precursor protein
Intracellular domain
Suggests
Complex
Model
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
Centre for Advanced Imaging Publications
 
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Created: Sun, 21 Jul 2013, 00:11:28 EST by System User on behalf of Institute for Molecular Bioscience