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C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site

Nature Structural Biology volume 4, pages 900–903 (1997)Cite this article

The crystal structure of human replication and transcription cofactor PC4CTD reveals a dimer with two single-stranded (ss)DNA binding channels running in opposite directions to each other. This arrangement suggests a role in establishment or maintenance of melted DMA at promoters or origins of replication.

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Authors and Affiliations

  1. Dept. of Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands

    Jeroen Brandsen, Jan Kroon & Piet Gros

  2. Laboratory for Physiological Chemistry, Utrecht University, The Netherlands

    Sebastiaan Werten & Peter C. van der Vliet

  3. Dept. of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands

    Sebastiaan Werten

  4. Laboratory for Molecular Biology-Genzentrum, Ludwig-Maximilians-University, Munich, Germany

    Michael Meisterernst

Authors
  1. Jeroen Brandsen
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  4. Michael Meisterernst
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  5. Jan Kroon
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  6. Piet Gros
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Brandsen, J., Werten, S., van der Vliet, P. et al. C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site. Nat Struct Mol Biol 4, 900–903 (1997). https://doi.org/10.1038/nsb1197-900

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