Figure 9. a) X-ray structure of the PKM2 tetramer with two equivalents of ML265 and four equivalents of 1,6-FBP bound.

Figure 9

a) X-ray structure of the PKM2 tetramer with two equivalents of ML265 and four equivalents of 1,6-FBP bound. ML265 binds at the dimer-dimer interface, termed A-A’. b) The sulfoxide and carbonyl group of ML265 form water mediated hydrogen bond networks the protein, while the aniline moiety forms a direct hydrogen bond with D354.

From: ML265: A potent PKM2 activator induces tetramerization and reduces tumor formation and size in a mouse xenograft model

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