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. 2020 Jun 23;7:77. doi: 10.3389/fmolb.2020.00077

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Copyright © 2020 Sun and Kekenes-Huskey.

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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(A) Two possible interaction models between S100A1 and actin-PEVK (AP) complex. In first model, half-saturated S100A1 does not bind to AP while in second model all apo S100A1, half-saturated S100A1 (Ca.S100A1) and fully-saturated S100A1 (2Ca.S100A1) bind to AP. (B) Fitting to experimental data from Yamasaki et al. (2011). (C) Comparison of predicted actin-PEVK binding as a function of wild-type (black) and glutathionylated (red) S100A1 at pCa = 7 (solid) and pCa = 4,5 (dashed). Assumed C85 glutathionylation leads to ~48 fold enhancement for S100A1's affinity to AP complex based on the PMF calculations.