Unified nomenclature for the winged helix/forkhead transcription factors.

  title={Unified nomenclature for the winged helix/forkhead transcription factors.},
  author={Klaus H. Kaestner and Walter Knochel and Daniel E Martinez},
  journal={Genes \& development},
  volume={14 2},
The winged helix/forkhead class of transcription factors is characterized by a 100-amino-acid, monomeric DNAbinding domain. The structure of the DNA-binding domain of one of the class members, hepatocyte nuclear factor 3 g (HNF3g), in a complex with a DNA target has been solved (Clark et al. 1993). The DNA-binding domain folds into a variant of the helix–turn–helix motif and is made up of three a helices and two characteristic large loops, or “wings.” Therefore, the DNA-binding motif has been… 

Figures from this paper

Winged-helix transcription factors and pancreatic development.

Molecular analyses have demonstrated that Foxa2 is an important regulator of the genes encoding Sur1, Kir6.2 and Schad (short chain L-3-hydroxyacyl-CoA dehydrogenase), mutation of which causes PHHI in humans.

Crystal Structure of the Human FOXK1a-DNA Complex and Its Implications on the Diverse Binding Specificity of Winged Helix/Forkhead Proteins*

The crystal structure of two DNA binding domains of ILF (FOXK1a) binding to a 16-bp DNA duplex containing a promoter sequence is reported, providing a new insight into how the DNA binding specificities of winged helix/forkhead proteins may be regulated by their less conserved regions.

DNA-binding specificity changes in the evolution of forkhead transcription factors

DNA-binding bispecificity suggests a previously undescribed source of modularity and flexibility in gene regulation and may play an important role in the evolution of transcriptional regulatory networks.

The structural basis for forkhead box family specificity revealed by the crystal structure of human FOXN1 in complex with DNA

The structure of FOXN1 is presented in complex with DNA at 1.6 Å resolution, in which the DNA sequence is recognised by a mixture of direct and water-mediated contacts provided by residues in an a-helix inserted in the DNA major groove (the recognition helix).

The crystal structure of human forkhead box N1 in complex with DNA reveals the structural basis for forkhead box family specificity

It is demonstrated that the C-terminal region ofFOXN1 is required for high-affinity DNA binding and that FOXN1 has a significantly reduced affinity for DNA that contains 5′-methylcytosine, which may have implications for the role of FOXN 1 in thymic involution.

FOXO transcription factors

Forkhead transcription factors: key players in development and metabolism.

Forkhead proteins are not among the largest transcription factor families, but display a remarkable functional diversity and are involved in a wide variety of biological processes.

Both the N-terminal Loop and Wing W2 of the Forkhead Domain of Transcription Factor Foxo4 Are Important for DNA Binding*

The results show that both N- and C-terminal regions of forkhead domain are important for stability of the FoxO4-DBD·DNA complex.



Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5

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 Å resolution and the transcription factor fold is very similar to the structure of histone H5.

Five years on the wings of fork head

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.

The sensitivity of the commonly used progressive multiple sequence alignment method has been greatly improved and modifications are incorporated into a new program, CLUSTAL W, which is freely available.