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Protein Engineering vol. 9 no. 8 pp. 631-635, 1996
© 1996 Oxford University Press

RESEARCH-ARTICLE

The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer

Hong-Wei Sun, Melissa Swope, Cinquina Craig, Sudhir Bedarkar, Jürgen Bernhagen1, Richard Bucala1 and Elias Lolis2

Department of Pharmacology, Yale University School of Medicine New Haven, CT 06510 1The Picower Institute for Medical Research Manhasset, NY 11030, USA

2To whom correspondence should be addressed

The subunit structure of human macrophage migration inhibitory factor (MIF) has been studied by preliminary X-ray analysis of wild-type and selenomethionine-MIF and dynamic light scattering. Crystal form I of MIF belongs to space group P212121 and is grown from 2 M ammonium sulfate at pH 8.5. A native data set has been collected to 2.4 Å resolution. Self-rotation studies and Vm values indicate that three molecules per asymmetric unit are present A data set to 2.8 Å resolution has been collected for crystal form II, which belongs to space group P3121 or P3221 and grows from 2 M ammonium sulfate, 2% polyethylene glycol (average molecular mass 400), 0.1 M HEPES, pH 7.5. Three, four, five or six monomers in the asymmetric unit are consistent with Vm values for this crystal form. Analysis of crystal form II containing selenomethionine-MIF indicates nine selenium sites are present per asymmetric unit. Dynamic light scattering of MIF suggests that the major form of the protein in solution is a trimer. The results of these studies are in contrast to previous reports indicating that MIF is a monomer or dimer. The subunit arrangement of MIF is similar to that of tumor necrosis factor and suggests that signal transduction might require trimerization of receptor subunits.

Keywords: crystallization/dynamic light scattering/macrophage/migration inhibitory factor/protein structure/X-ray diffraction

Received November 27, 1995; accepted March 3, 1996.


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