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. 2019 Mar 21;20(6):1444. doi: 10.3390/ijms20061444

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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The saturation isotherms of [³H]-PK 11195 binding to reconstituted rec-mTSPO in proteoliposomes: (A) the wild type (WT) rec-mTSPO, (B) mutants Y34 (F and S opened and closed squares, respectively), (C) deletion mutants (Δ41–51 and Δ153–169 open and closed diamonds, respectively) and (D) mutant F100A, double mutants Y34F/F100A and Y34F/F99A (open and closed triangles and filled red circles, respectively). The lines represent the best-fit regression curves. The dashed line in panels (B–D) corresponds to that of WT presented in panel (A).