Open AccessThe structure of the unstructured: mosaic of tau protein linear motifs obtained by high-resolution techniques and molecular simulation
Author(s) -
Ondrej Cehlár,
Olga Bagarova,
Lenka Hornakova,
Rostislav Škrabana
Publication year - 2021
Publication title -
general physiology and biophysics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.376
H-Index - 39
eISSN - 1338-4325
pISSN - 0231-5882
DOI - 10.4149/gpb_2021031
Subject(s) - tau protein , chemistry , crystallography , protein structure , molecular dynamics , biophysics , physics , biology , computational chemistry , biochemistry , medicine , disease , pathology , alzheimer's disease
Intrinsically disordered proteins are flexible molecules with important physiological functions. Their mode of action often involves short segments, called linear motifs, which may exhibit distinct structural propensities. Tau is intrinsically disordered, microtubule-associated protein involved in the pathogenesis of various tauopathies. In this review we analyze the collection of 3D structures of tau local linear motifs gained from the deposited structures of tau complexes with various binding partners as well as of tau-tau complexes; determined by X-ray and electron crystallography, single-particle electron microscopy, NMR spectroscopy and molecular dynamics simulations. Insights into the partially stabilized conformations of tau linear motifs are valuable for understanding the physiological and pathological processes involving tau protein.