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. 2009 Sep 23;284(47):32425–32433. doi: 10.1074/jbc.M109.047092

FIGURE 5.

FIGURE 5.

In silico model of PEITC bound to the tautomerase active site of MIF via covalent modification of the N-terminal proline residue. The MIF homotrimer is shown with PEITC (yellow) docked in one of the tautomerase active sites. MIF without PEITC bound is shown in magenta (PDB code 3B9S). Conformational shifts of the catalytic proline by 2 Å (arrow 1) and lysine 32 by 1.6 Å (arrow 2) are highlighted. A zoom image of the highlighted region in A is shown in B.