Skip to main content
. Author manuscript; available in PMC: 2015 Dec 1.
Published in final edited form as: J Biomol Screen. 2014 Aug 25;19(10):1338–1349. doi: 10.1177/1087057114547232

Figure 4.

Figure 4

Model for how disruption of Tau tertiary structure may facilitate Tau–Fyn SH3 interactions. Location of β-strands are approximate based on a published map of Tau secondary structure elements36. Under normal conditions, interactions between β-strands may help maintain Tau in a conformation that reduces access to the proline-rich domain. Phosphorylation may disrupt interactions between β-strands (right), opening the paperclip conformation of Tau and facilitating Fyn binding to the proline-rich domain.