Structural highlights
Function
[FOXQ1_RAT] Plays a role in hair follicle differentiation (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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.,Sheng W, Rance M, Liao X Biochemistry. 2002 Mar 12;41(10):3286-93. PMID:11876636[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sheng W, Rance M, Liao X. 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. Biochemistry. 2002 Mar 12;41(10):3286-93. PMID:11876636
