Crystal structure of the macrophage migration inhibitory factor from rat liver

被引:176
作者
Suzuki, M
Sugimoto, H
Nakagawa, A
Tanaka, I
Nishihira, J
Sakai, M
机构
[1] HOKKAIDO UNIV,GRAD SCH SCI,DIV BIOL SCI,SAPPORO,HOKKAIDO 060,JAPAN
[2] HOKKAIDO UNIV,SCH MED,CENT RES INST,SAPPORO,HOKKAIDO 060,JAPAN
来源
NATURE STRUCTURAL BIOLOGY | 1996年 / 3卷 / 03期
关键词
D O I
10.1038/nsb0396-259
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The tertiary structure of the macrophage migration inhibitory factor (MIF) from rat liver (12,300 M(r)) is presented at 2.2 Angstrom 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.
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收藏
页码:259 / 266
页数:8
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