Recognition of distorted DNA structures by HMG domains

Curr Opin Struct Biol. 2000 Feb;10(1):102-9. doi: 10.1016/s0959-440x(99)00056-1.

Abstract

Recent biochemical and structural studies have shown that the preferential recognition of distorted DNA structures, including DNA bulges, four-way junctions and cis-platinated DNA, by HMG domains is dependent on residues immediately preceding the second alpha helix of the L-shaped HMG domain.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • DNA Damage*
  • DNA Repair
  • High Mobility Group Proteins / chemistry
  • High Mobility Group Proteins / metabolism*
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation*
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Nucleic Acid
  • Substrate Specificity

Substances

  • High Mobility Group Proteins
  • Macromolecular Substances