作者: Kateřina Melková , Vojtěch Zapletal , Subhash Narasimhan , Séverine Jansen , Jozef Hritz
DOI: 10.3390/BIOM9030105
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摘要: The stability and dynamics of cytoskeleton in brain nerve cells are regulated by microtubule associated proteins (MAPs), tau MAP2. Both intrinsically disordered involved multiple molecular interactions important for normal physiology pathology chronic neurodegenerative diseases. Nuclear magnetic resonance cryo-electron microscopy recently revealed propensities MAPs to form transient local structures long-range contacts the free state, conformations adopted complexes with microtubules filamentous actin, as well pathological aggregates. In this paper, we compare longest, 441-residue isoform (tau40), a 467-residue MAP2, known MAP2c. For both molecules, present structural motifs conformational analysis experimental data obtained soluble forms proteins. We show that many short sequence exhibit features linked functional properties, manifested specific interactions. can be therefore classified recognition elements tau40 Their further post-translational modifications, particular phosphorylation. structure-function also explains differences between biological activities