Structure of the NF-kappa B p50 homodimer bound to DNA

Nature. 1995 Jan 26;373(6512):311-7. doi: 10.1038/373311a0.

Abstract

The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-barrel domains that grip DNA in the major groove. Both domains contact the DNA backbone. The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the carboxy-terminal dimerization domain bears the site of I-kappa B interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Computer Graphics
  • Crystallography, X-Ray
  • DNA / chemistry*
  • DNA / metabolism
  • Humans
  • Molecular Sequence Data
  • NF-kappa B / chemistry*
  • NF-kappa B / metabolism
  • NF-kappa B p50 Subunit
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins c-rel
  • Recombinant Proteins / chemistry

Substances

  • NF-kappa B
  • NF-kappa B p50 Subunit
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-rel
  • Recombinant Proteins
  • DNA