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Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways
Abstract Isoforms of microtubule associated protein 2 (MAP2) differ from their homologue Tau in the sequence and interactions of the N-terminal region. Binding of the N-terminal region of MAP2c (N-MAP2c) to the dimerization/docking domains of the regulatory subunit RIIα of cAMP-dependent protein kinase (RIIDD2) and to the Src-homology domain 2 of growth factor receptor‐bound protein 2 (Grb2) have been described long time ago.
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