1cqt
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(New page: 200px<br /> <applet load="1cqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cqt, resolution 3.20Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:18, 12 November 2007
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CRYSTAL STRUCTURE OF A TERNARY COMPLEX CONTAINING AN OCA-B PEPTIDE, THE OCT-1 POU DOMAIN, AND AN OCTAMER ELEMENT
Overview
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.
About this Structure
1CQT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface., Chasman D, Cepek K, Sharp PA, Pabo CO, Genes Dev. 1999 Oct 15;13(20):2650-7. PMID:10541551
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