[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.