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Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer
Author(s) -
Neves João Filipe,
Petrvalská Olivia,
Bosica Francesco,
Cantrelle FrançoisXavier,
Merzougui Hamida,
O'Mahony Gavin,
Hanoulle Xavier,
Obšil Tomáš,
Landrieu Isabelle
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15574
Subject(s) - phosphorylation , tau protein , dimer , chemistry , binding site , binding selectivity , crystallography , biophysics , biochemistry , biology , alzheimer's disease , medicine , disease , organic chemistry , pathology
Pharmacological modulation of the 14‐3‐3/Tau interaction has interest in drug discovery projects related to Alzheimer’s disease mitigation. Biophysical methods were used to define the interface, stoichiometry, and affinity characterizing the binding of 14‐3‐3 to full‐length phosphorylated Tau protein. We concluded that the small binding interface and the interaction of moderate affinity make the interface likely druggable for inhibition.