1CQT

CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT

Summary for 1CQT

• Entry DOI: 10.2210/pdb1cqt/pdb
• Descriptor: DNA (5'-D(*TP*GP*TP*AP*TP*GP*CP*AP*AP*AP*TP*AP*AP*GP*G)-3'), DNA (5'-D(*AP*CP*CP*TP*TP*AP*TP*TP*TP*GP*CP*AP*TP*AP*C)-3'), POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 1, ... (4 entities in total)
• Functional Keywords: pou domain, protein-dna complex, oct1, oca-b, protein-dna interface, gene regulation/dna, gene regulation-dna complex
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P14859 Q16633
• Total number of polymer chains: 8
• Total formula weight: 65618.11

Authors

Chasman, D.I.,Cepek, K.,Sharp, P.A.,Pabo, C.O. (deposition date: 1999-08-11, release date: 1999-11-15, Last modification date: 2024-02-07)

Primary citation

Chasman, D.,Cepek, K.,Sharp, P.A.,Pabo, C.O.
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 Dev., 13:2650-2657, 1999

PubMed Abstract: 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: 10541551
DOI: 10.1101/gad.13.20.2650

Experimental method

X-RAY DIFFRACTION (3.2 Å)