The Tautomerase Active Site of Macrophage Migration Inhibitory factor is a Potential Target for Discovery of Novel Anti-inflammatory Agents
Lubetsky, J.B., Dios, A., Han, J., Aljabari, B., Ruzsicska, B., Mitchell, R., Lolis, E., Al-Abed, Y.(2002) J Biol Chem 277: 24976-24982
- PubMed: 11997397 
- DOI: https://doi.org/10.1074/jbc.M203220200
- Primary Citation of Related Structures:  
1LJT - PubMed Abstract: 
Macrophage migration inhibitory factor (MIF) is an immunoregulatory protein that is a potential therapeutic target for a number of inflammatory diseases. Evidence exists that an unexpected catalytic active site of MIF may have a biological function. To gain further insight into the role of the catalytic active site, a series of mutational, structural, and biological activity studies were performed. The insertion of an alanine between Pro-1 and Met-2 (PAM) abolishes a non-physiological catalytic activity, and this mutant is defective in the in vitro glucocorticoid counter-regulatory activity of MIF. The crystal structure of MIF complexed to (S,R)-3-(4-hydroxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester (ISO-1), an inhibitor of MIF d-dopachrome tautomerase activity, reveals that ISO-1 binds to the same position of the active site as p-hydroxyphenylpyruvic acid, a substrate of MIF. ISO-1 inhibits several MIF biological activities, further establishing a role for the catalytic active site of MIF.
Organizational Affiliation: 
Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.