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. 2018 Nov 14;11:421. doi: 10.3389/fnmol.2018.00421

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Copyright © 2018 Lasorsa, Malki, Cantrelle, Merzougui, Boll, Lambert and Landrieu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Assignment of Tau (210–240) proline residues. (A) Domain composition of the largest isoform of the neuronal Tau protein. P1 and P2 are the proline-rich regions. Tau (210–240) sequence is shown as part of the PRD. The proline residues are indicated in bold characters. The canonical SH3 class I and II binding motifs are underlined and the consensus motifs are given below. PPII.1 and PPII.2 are PPII helix motif class I and II, respectively. (B) Assigned 2D HA(CA)N spectrum of the prolines in Tau (210–240) peptide at 20°C.