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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.

Chasman D, Cepek K, Sharp PA, Pabo CO
Genes Dev 13 2650-7 (1999)
Cited: 62 times
EuropePMC logo PMID: 10541551

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.

Reviews - 1cqt mentioned but not cited (1)

  1. Homeodomain revisited: a lesson from disease-causing mutations. Chi YI. Hum Genet 116 433-444 (2005)

Articles - 1cqt mentioned but not cited (7)

  1. 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 13 2650-2657 (1999)
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Related citations provided by authors (1)

  1. Crystal Structure of the Oct-1 POU Domain Bound to an Octamer Site: DNA Recognition with Tethered DNA-Binding Modules. Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO Cell 77 21- (1994)

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