Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element

Nat Struct Biol. 2003 Oct;10(10):800-6. doi: 10.1038/nsb981. Epub 2003 Aug 31.


DNA binding by NFAT1 as a dimer has been implicated in the activation of host and viral genes. Here we report a crystal structure of NFAT1 bound cooperatively as a dimer to the highly conserved kappa B site from the human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR). This structure reveals a new mode of dimerization and protein-DNA recognition by the Rel homology region (RHR) of NFAT1. The two NFAT1 monomers form a complete circle around the kappa B DNA through protein-protein interactions mediated by both their N- and C-terminal subdomains. The major dimer interface, formed by the C-terminal domain, is asymmetric and substantially different from the symmetric dimer interface seen in other Rel family proteins. Comparison to other NFAT structures, including NFAT5 and the NFAT1-Fos-Jun-ARRE2 complex, reveals that NFAT1 adopts different conformations and its protein surfaces mediate distinct protein-protein interactions in the context of different DNA sites.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • Dimerization
  • HIV Long Terminal Repeat / genetics*
  • HIV Long Terminal Repeat / physiology
  • Humans
  • Molecular Sequence Data
  • NFATC Transcription Factors
  • Nuclear Proteins*
  • Protein Structure, Tertiary
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism


  • DNA-Binding Proteins
  • NFATC Transcription Factors
  • NFATC2 protein, human
  • Nuclear Proteins
  • Transcription Factors

Associated data

  • PDB/1P7H