The MSP domain of MOSPD2 binds the FFAT motif with an affinity in the micromolar range The MSP domain of MOSPD2 binds the FFAT motif with an affinity in.

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The MSP domain of MOSPD2 binds the FFAT motif with an affinity in the micromolar range The MSP domain of MOSPD2 binds the FFAT motif with an affinity in the micromolar range A–HSurface plasmon resonance analysis of the MSP domain of MOSPD2, VAP‐A, or VAP‐B binding onto immobilized FFAT peptide. Representative sensorgrams resulting from the interaction between the MSP domain of MOSPD2 (A), VAP‐A (B), or VAP‐B (C) injected at different concentrations, and the FFAT peptide. No binding was detected when the RD/LD mutant MSP domain of MOSPD2 was injected onto the FFAT peptide (G), or when the wild‐type MSP domain of MOSPD2 was injected onto the immobilized control peptide (H). Binding curves display the SPR signal (RU) as a function of time. Concentrations printed in bold indicate samples measured three times. Samples with no protein (0 μM concentration) were measured two times. (D) Steady‐state analysis of the FFAT peptide/MSP domain of MOSPD2 interaction: Equilibrium responses (Req) extracted from panel (A) were plotted as a function of the MSP domain of MOSPD2 concentration, and fitted with a 1:1 binding model. (E, F) Steady‐state analysis of the FFAT peptide/MSP domain of VAP‐A (E) or VAP‐B (F) interaction: equilibrium responses (Req) extracted from panel (A) were plotted as a function of dimeric VAP concentration and fitted with a 1:1 binding model. Thomas Di Mattia et al. EMBO Rep. 2018;19:e45453 © as stated in the article, figure or figure legend