Crystal structure of macrophage migration inhibitory factor from human lymphocyte at 2.1 A resolution.
The three-dimensional structure of the macrophage migration inhibitory factor (MIF) from human lymphocytes has been determined by X-ray crystallography at 2.1 A resolution. The structure was solved by a molecular replacement technique using the coordinates of rat MIF. The molecule forms a trimer structure similar to the rat MIF. However, unlike the rat MIF whose C-terminal tail (residues 104-114) is disordered in the crystal, human MIF has a definite main-chain conformation up to the C-terminal end. These eleven residues create two more beta-strands and join to the inter-subunit beta-sheet, which contribute to forming a trimer structure. Thus, the trimer structure consists of three seven-stranded beta-sheets surrounded by six alpha-helices. Each beta-sheet is comprised of beta-strands from each of the three monomers. This architecture is almost identical to 5-carboxymethyl-2-hydroxymuconate isomerase (CHMI) and is related to the E. coli signal transducing protein PII.
Sugimoto
H
H
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Suzuki
M
M
Nakagawa
A
A
Tanaka
I
I
Nishihira
J
J
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray / Q000379:methods; D006801:Humans; D008263:Macrophage Migration-Inhibitory Factors / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D013601:T-Lymphocytes / Q000737:chemistry
D008263:Macrophage Migration-Inhibitory Factors