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Crystal structure of the macrophage migration inhibitory factor from rat liver
M Suzuki1, H Sugimoto, A Nakagawa
1Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Nature Structural Biology
|March 1, 1996
Abstract:
The tertiary structure of the macrophage migration inhibitory factor (MIF) from rat liver (12,300 Mr) is presented at 2.2 A resolution. Each monomer consists of two beta/alpha/beta motifs aligned in quasi two-fold symmetry, comprising a domain consisting of a four-stranded mixed beta-sheet and two antiparallel alpha-helices. The protein exists as a trimer in the crystal. An extra beta-strand that is almost perpendicular to the other beta-strands joins to the beta-sheet of the neighbouring monomer in the trimer. Unexpected similarities were detected between MIF and two kinds of isomerase.