Figure 7: Structure analysis of the kinase domain of murine IRE1α. | Nature Communications

Figure 7: Structure analysis of the kinase domain of murine IRE1α.

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

Figure 7

(a) Ribbons’ representation of IRE1α kinase domains highlighting regulatory (yellow) and catalytic (red) spine alignments. All yeast structures solved to date display productive alignment of spines (right), while HAA-bound murine IRE1α structures and the dephospho-human IRE1α structure adopt non-productive alignments of the regulatory spine. PDB code and the respective ligand engaging the kinase-active site are indicated. (b) Zoom-in view of the kinase-active site of murine IRE1α superimposed on yeast IRE1 (PDB 2RIO) highlighting the displaced position of helix αC. (c) Zoom-in view of the projected back-to-back dimer interface of murine IRE1α (only one protomer shown) superimposed on the yeast IRE1 back-to-back dimer (PDB 2RIO) highlighting the physical link between helix αC and the back-to-back dimer interface. Side chains composing an essential intra-dimer salt bridge and the subdomain III glutamate side chain are shown as sticks.

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