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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.

Genes & development | Oct 15, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10541551

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 RIS Download

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