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 7
Mass-spectrometric analyses of the preparative-scale covalent reactions of different versions of GPX4 with ML162. (a) GPX4^WT, outcome of approach 1 [50 µM GPX4^WT incubated for 35 min with a fivefold molar excess of ML162 (racemate)], revealing a mixture of unmodified, singly modified and doubly modified GPX4. (b) GPX4^WT, approach 2 [50 µM GPX4^WT incubated for 4 h with a 50-fold molar excess of ML162 (racemate)], resulting in homogenously doubly modified protein. (c) Large-scale reaction of GPX4^C66S with (S)-ML162, indicating complete turnover of the protein to the singly modified state upon incubation of 50 µM protein with 125 µM ligand for 30 min.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798320016125

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