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. 2021 Mar 19;12:1718. doi: 10.1038/s41467-021-21960-4

Fig. 5. PKM2 citrullination diminishes allosteric inhibition by Phe/Ala/Trp.

Fig. 5

a Close up view of free Ser and Phe interactions within the free amino acid binding pocket in the Apo, R-active and T-inactive states with a superposition of the three structures. All residues displayed are shown as sticks. In the superposition, the peptide bearing R43 is represented as ribbon to show the allosteric changes created upon Phe binding. Salt bridges and hydrogen bonds are shown as dashed lines. For clarity, the side chain of Phe 470, which stacks on R106 side chain, is not displayed. PDB data sets are as described in Supplementary Fig. 3. b ECAR values in absence of Ser after CHD4 silencing or PAD1/3 expression in 501Mel or MM117 cells; NM = normal medium. c ECAR values in presence of exogenous Ser with or without CHD4 silencing in 501Mel cells. d, e ECAR values in presence of exogenous Trp or Phe with or without CHD4 silencing or PAD1/3 expression in 501Mel cells. f ECAR values in presence of exogenous Phe with or without CHD4 silencing in MM117 cells. g ECAR values in presence of exogenous Ala with or without PAD1/3 expression in 501Mel cells. h, i PKM2 enzymatic activity in cell extracts supplemented with the indicated concentrations of Trp and Phe or PBS as control. In all experiments ECAR values and PKM2 enzymatic activity were determined from n = 3 biological replicates with 6 technical replicates for each N for ECAR. n = 3 biological replicates. and unpaired t-test with two tailed p-value analyses and confidence interval 95% were performed by Prism 5. p-Values: *p < 0.05; **p < 0.01; ***p < 0.001. Data are mean ± SEM. Values for PKM2 enzymatic activity were determined by Prism 5 using a 2-way ANOVA test.