Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162

Moosmayer, D.; Hilpmann, A.; Hoffmann, J.; Schnirch, L.; Zimmermann, K.; Badock, V.; Furst, L.; Eaton, J.K.; Viswanathan, V.S.; Schreiber, S.L.; Gradl, S.; Hillig, R.C.

doi:10.1107/S2059798320016125

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
(a) Mass-spectrometric analyses of the covalent reaction of GPX4^WT with ML162 (racemate). Shown are deconvoluted mass spectra after 10, 20 and 30 min of incubating 50 µM GPX4^WT with 125 µM ML162 (racemate). (b, c) Mass-spectrometric analyses of the covalent reaction of GPX4^WT with (b) the pure (S)-enantiomer and (c) the pure (R)-enantiomer. A time-course analysis is shown of the observed GPX4 species (unmodified or onefold, twofold or threefold covalently modified with ML162) found at the given time points for the ligand:protein ratios given in the box.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 77| Part 2| February 2021| Pages 237-248

https://doi.org/10.1107/S2059798320016125

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