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Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface.

We have determined the crystal structure, at 3.2 A, of a ternary complex containing an OCA-B peptide, the Oct-1 POU domain, and an octamer DNA site. The OCA-B peptide binds in the major groove near the center of the octamer site, and its polypeptide backbone forms a pair of hydrogen bonds with the adenine base at position 5 of the octamer DNA. Numerous protein-protein contacts between the OCA-B peptide and the POU domain are also involved in the ternary complex. In particular, the hydrophobic surface from a short alpha-helix of OCA-B helps to stabilize the complex by binding to a hydrophobic pocket on the POU-specific domain. The structure of this ternary complex is consistent with previous biochemical studies and shows how peptide-DNA and peptide-protein contacts from OCA-B provide structural and functional specificity in the regulation of immunoglobulin transcription.

Pubmed ID: 10541551


  • Chasman D
  • Cepek K
  • Sharp PA
  • Pabo CO


Genes & development

Publication Data

October 15, 1999

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM31471
  • Agency: NCI NIH HHS, Id: P01-CA42063
  • Agency: NCI NIH HHS, Id: P30-CA14051

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • DNA
  • DNA-Binding Proteins
  • Host Cell Factor C1
  • Humans
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Octamer Transcription Factor-1
  • Peptide Fragments
  • Protein Conformation
  • Recombinant Proteins
  • Static Electricity
  • Trans-Activators
  • Transcription Factors