CO-CRYSTAL STRUCTURE OF THE HNF-3/FORK HEAD DNA-RECOGNITION MOTIF RESEMBLES HISTONE-H5

被引:1141
作者
CLARK, KL
HALAY, ED
LAI, ES
BURLEY, SK
机构
[1] ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
[2] ROCKEFELLER UNIV, HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA
[3] MEM SLOAN KETTERING CANC CTR, CELL BIOL & GENET PROGRAM, NEW YORK, NY 10021 USA
[4] MEM SLOAN KETTERING CANC CTR, ENDOCRINOL SERV, NEW YORK, NY 10021 USA
关键词
D O I
10.1038/364412a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The three-dimensional structure of an HNF-3/fork head DNA-recognition motif complexed with DNA has been determined by X-ray crystallography at 2.5 angstrom resolution. This alpha/beta protein binds B-DNA as a monomer, through interactions with the DNA backbone and through both direct and water-mediated major and minor groove base contacts, inducing a 13-degrees bend. The transcription factor fold is very similar to the structure of histone H5. In its amino-terminal half, three alpha-helices adopt a compact structure that presents the third helix to the major groove. The remainder of the protein includes a twisted, antiparallel beta-structure and random coil that interacts with the minor groove.
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页码:412 / 420
页数:9
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