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

Citation
Kl. Clark et al., CO-CRYSTAL STRUCTURE OF THE HNF-3 FORK HEAD DNA-RECOGNITION MOTIF RESEMBLES HISTONE-H5/, Nature, 364(6436), 1993, pp. 412-420
Citations number
49
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Volume
364
Issue
6436
Year of publication
1993
Pages
412 - 420
Database
ISI
SICI code
0028-0836(1993)364:6436<412:CSOTHF>2.0.ZU;2-X
Abstract
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 m onomer, through interactions with the DNA backbone and through both di rect and water-mediated major and minor groove base contacts, inducing a 13-degrees bend. The transcription factor fold is very similar to t he structure of histone H5. In its amino-terminal half, three alpha-he lices adopt a compact structure that presents the third helix to the m ajor groove. The remainder of the protein includes a twisted, antipara llel beta-structure and random coil that interacts with the minor groo ve.