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. 2015 Jul 1;2:36. doi: 10.3389/fmolb.2015.00036

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Copyright © 2015 Lamprakis, Stocker and Cascella.

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) or licensor 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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Comparison of the α-TTP-α-Tol-PI(3,4)P₂ complex n differentstates. (A) the scaffold of the partially-bound structure from X-ray scattering [PDB: 3W67 (Kono et al., 2013), in green cartoon], is superimposed to the fully bound structure obtained from our MD simulations (orange cartoon) and to the closed X-ray structure with fully bound α-Tol [PDB: 1OIP (Meier et al., 2003)] (blue). (B) the inset report a zoom of the mobile gate helix (N198-K217) and the G162-L183 segment with which the mobile gate is in contact in closed structures. (C) Contact maps between the G162-L183 and the N198-K217 segments in the intermediate state captured in PDB: 3W67 (Kono et al., 2013) (C1), in the α-TTP-α-Tol complex (PDB: 1OIP, Meier et al., 2003, C2), and in the relaxed structure from MD simulations for the α-TTP-PI(3,4)P₂ complex (C3) and for the α-TTP-PI(4,5)P₂ complex (C4).