Structure comparison of two conserved HNF-3/fkh proteins HFH-1 and genesis indicates the existence of folding differences in their complexes with a DNA binding sequence.
The hepatocyte nuclear factor 3 (HNF-3)/fork head (fkh) family contains a large number of transcription factors that recognize divergent DNA sequences via a winged helix binding motif. HNF-3/fkh proteins show a broad profile of DNA sequence-specificity in which one DNA sequence can be recognized by more than one HNF-3/fkh protein and each individual HNF-3/fkh protein has several DNA binding sequences. In this study, heteronuclear NMR methods were used to study the structures of the DNA binding domain of a conserved winged helix protein HFH-1 and its DNA complexes. The structural comparison of winged helix proteins HFH-1 and Genesis and their DNA complexes indicates that even two highly conserved HNF-3 family members can adopt different local structures when they contact an identical DNA binding sequence, while one of these two HNF-3 proteins seems to adopt only slightly different structures on different DNA binding sites.
Sheng
Wanyun
W
Department of Biochemistry and Molecular Biology, College of Medicine, University of Illinois at Chicago, 1835 West Polk Street, Chicago, Illinois 60612-4316, USA.
Rance
Mark
M
Liao
Xiubei
X
D000595:Amino Acid Sequence; D001483:Base Sequence; D004247:DNA; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000502:physiology; D051858:Forkhead Transcription Factors; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry* / Q000502:physiology; D015534:Trans-Activators / Q000737:chemistry* / Q000502:physiology
D004268:DNA-Binding Proteins; D051858:Forkhead Transcription Factors; C491100:Foxd3 protein, rat; D012097:Repressor Proteins; D015534:Trans-Activators; D004247:DNA