Figure 3: Crystal structure of IRE1α bound to MKC9989. | Nature Communications

Figure 3: Crystal structure of IRE1α bound to MKC9989.

From: Structure and mechanism of action of the hydroxy–aryl–aldehyde class of IRE1 endoribonuclease inhibitors

Figure 3

(a) Ribbons representation of a face-to-face dimer configuration of IRE1α in complex with Mg2+/ADP and MKC9989. ADP engaging the kinase-active site and MKC9989 engaging the RNase-active site are shown as sticks and highlighted by red boxes. For comparison, the dimer configurations adopted by human IRE1α (PDB 3P23) and yeast IRE1 (PDB 3LJ0) are shown at right. (b) Ribbons’ stereo representation of MKC9989 engaging the RNase-active site of IRE1α. Invariant active site residues, Lys907 and other conserved residues in the binding pocket are coloured purple, yellow and pink, respectively. Lys907 forms a Schiff base to the aldehyde moiety of MKC9989. (c) Zoom in surface view of the IRE1α–MKC9989 complex coloured as in b. (d) Schematic of contact residues and notable interactions mediating MKC9989 binding to IRE1α.

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