Structure of NF-kappa B p50 homodimer bound to a kappa B site

Nature. 1995 Jan 26;373(6512):303-10. doi: 10.1038/373303a0.

Abstract

The 2.3-A crystal structure of the transcription factor NK-kappa B p50 homodimer bound to a palindromic kappa B site reveals that the Rel homology region folds into two distinct domains, similar to those in the immunoglobulin superfamily. The p50 dimer envelopes an undistorted B-DNA helix, making specific contacts along the 10-base-pair kappa B recognition site mainly through loops connecting secondary structure elements in both domains. The carboxy-terminal domains form a dimerization interface between beta-sheets using residues that are strongly conserved in the Rel family.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Computer Graphics
  • Crystallography, X-Ray
  • DNA / chemistry*
  • Drosophila
  • Humans
  • Immunoglobulins / chemistry
  • Mice
  • 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 / metabolism
  • Proto-Oncogene Proteins c-rel
  • RNA
  • Sequence Homology, Amino Acid

Substances

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