Co-crystal structure of the HNF-3/ fork head DNA-recognition motif resembles histone H5
作者： Kirk L. Clark , Elaine D Halay , Eseng Lai , Stephen K Burley
DOI: 10.1038/364412A0
关键词: Winged Helix 、 DNA 、 Random coil 、 Stereochemistry 、 Protein structure 、 Biology 、 Fork head domain 、 Forkhead Transcription Factors 、 Antiparallel (biochemistry) 、 DNA-binding protein
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 A resolution. This alpha/beta protein binds B-DNA as a monomer, through interactions the backbone and both direct water-mediated major minor groove base contacts, inducing 13 degrees bend. transcription factor fold is very similar to histone H5. In its amino-terminal half, three alpha-helices adopt compact that presents third helix groove. remainder includes twisted, antiparallel beta-structure random coil interacts
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