Solution structure and dynamics of the DNA-binding domain of the adipocyte-transcription factor FREAC-11

J Mol Biol. 2000 Feb 18;296(2):351-9. doi: 10.1006/jmbi.1999.3476.

Abstract

Transcription factors of the forkhead type share a highly conserved DNA-binding domain of about 100 amino acid residues. FREAC-11, expressed in adipocytes, belongs to this class. Here, we report on NMR studies that established the three-dimensional structure of the FREAC-11, DNA-binding domain. Although apparent similarities to the structures of other members within the forkhead family are observed, the structure also reveals some remarkable differences. Along with the complementary dynamics, the data provide insight into the fundamentals of sequence specificity within a highly conserved motif.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipose Tissue / chemistry*
  • Amino Acid Sequence
  • Binding Sites
  • DNA / genetics
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Forkhead Transcription Factors
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Nuclear Proteins / chemistry
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Solutions
  • Substrate Specificity
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism*

Substances

  • DNA-Binding Proteins
  • FREAC-11 protein, human
  • Forkhead Transcription Factors
  • Nuclear Proteins
  • Peptide Fragments
  • Solutions
  • Transcription Factors
  • DNA

Associated data

  • PDB/1D54