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CO-CRYSTAL STRUCTURE OF THE HNF-3/FORK HEAD DNA-RECOGNITION MOTIF RESEMBLES HISTONE-H5
Author(s): CLARK KL, HALAY ED, LAI ES, BURLEY SK
Source: NATURE    Volume: 364    Issue: 6436    Pages: 412-420    Published: JUL 29 1993  
Times Cited: 706     References: 49     
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 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.
Document Type: Article
Language: English
Addresses:
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
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: LP640
ISSN: 0028-0836
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