2M38

PTB domain of AIDA1

Summary for 2M38

• Entry DOI: 10.2210/pdb2m38/pdb
• NMR Information: BMRB: 17934
• Descriptor: Ankyrin repeat and sterile alpha motif domain-containing protein 1B (1 entity in total)
• Functional Keywords: phosphotyrosine binding domain, peptide binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm . Isoform 2: Nucleus. Isoform 3: Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Isoform 4: Nucleus. Isoform 6: Nucleus: Q7Z6G8
• Total number of polymer chains: 1
• Total formula weight: 17065.56

Authors

Donaldson, L. (deposition date: 2013-01-14, release date: 2013-01-23, Last modification date: 2024-05-15)

Primary citation

Smirnova, E.,Shanbhag, R.,Kurabi, A.,Mobli, M.,Kwan, J.J.,Donaldson, L.W.
Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein.
Plos One, 8:e65605-e65605, 2013

PubMed 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.

PubMed: 23799029
DOI: 10.1371/journal.pone.0065605

Experimental method

SOLUTION NMR