The tertiary structure of the macrophage migration inhibitory factor (MIF) from rat liver (12,300 Mr) is presented at 2.2 Å resolution. Each monomer consists of two β/α/β motifs aligned in quasi two-fold symmetry, comprising a domain consisting of a four-stranded mixed β-sheet and two antiparallel α-helices. The protein exists as a trimer in the crystal. An extra β-strand that is almost perpendicular to the other β-strands joins to the β-sheet of the neighbouring monomer in the trimer. Unexpected similarities were detected between MIF and two kinds of isomerase.
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Suzuki, M., Sugimoto, H., Nakagawa, A. et al. Crystal structure of the macrophage migration inhibitory factor from rat liver. Nat Struct Mol Biol 3, 259–266 (1996). https://doi.org/10.1038/nsb0396-259
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