Winged helix proteins

Curr Opin Struct Biol. 2000 Feb;10(1):110-6. doi: 10.1016/s0959-440x(99)00057-3.

Abstract

The winged helix proteins constitute a subfamily within the large ensemble of helix-turn-helix proteins. Since the discovery of the winged helix/fork head motif in 1993, a large number of topologically related proteins with diverse biological functions have been characterized by X-ray crystallography and solution NMR spectroscopy. Recently, a winged helix transcription factor (RFX1) was shown to bind DNA using unprecedented interactions between one of its eponymous wings and the major groove. This surprising observation suggests that the winged helix proteins can be subdivided into at least two classes with radically different modes of DNA recognition.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans Proteins
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / physiology
  • Helix-Loop-Helix Motifs*
  • Helminth Proteins / chemistry
  • Helminth Proteins / physiology
  • Hepatocyte Nuclear Factor 3-gamma
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / physiology
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • Receptor, Insulin / chemistry
  • Receptor, Insulin / physiology
  • Regulatory Factor X Transcription Factors
  • Regulatory Factor X1
  • Regulatory Sequences, Nucleic Acid
  • Sequence Alignment
  • Structure-Activity Relationship
  • Transcription Factors / chemistry*
  • Transcription Factors / physiology

Substances

  • Caenorhabditis elegans Proteins
  • DNA-Binding Proteins
  • Foxa3 protein, mouse
  • Helminth Proteins
  • Nuclear Proteins
  • Regulatory Factor X Transcription Factors
  • Regulatory Factor X1
  • Rfx1 protein, mouse
  • Transcription Factors
  • Hepatocyte Nuclear Factor 3-gamma
  • DAF-2 protein, C elegans
  • Receptor, Insulin