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. 2012 Mar 21;287(20):16267–16275. doi: 10.1074/jbc.M112.346411

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — Structural basis for off-target activation of PR. A, the human PR (hPR)-MOF complex (white; Protein Data Bank code 1SR7) superimposed on the AncGR2-MOF complex (red). PR residue Phe-794 maintains space for the 17α-furoate moiety and contributes a hydrophobic interaction via the aromatized side chain (15). PR residues ⁷⁹¹ESSF⁷⁹⁴ on H7 appear to play a key role in allowing strong MOF binding by positioning the H6-H7 loop and H7 via a conserved Glu-791–Ser-793 H-bond. B, this motif is strictly conserved among extant PRs but is not present in AncSR2.