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Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity

Author

Listed:
  • Stanley S. Ng

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Kathryn L. Kavanagh

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Michael A. McDonough

    (University of Oxford, Mansfield Road, Oxford OX1 3TA, UK)

  • Danica Butler

    (University of Oxford, Mansfield Road, Oxford OX1 3TA, UK)

  • Ewa S. Pilka

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Benoit M. R. Lienard

    (University of Oxford, Mansfield Road, Oxford OX1 3TA, UK)

  • James E. Bray

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Pavel Savitsky

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Opher Gileadi

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Frank von Delft

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Nathan R. Rose

    (University of Oxford, Mansfield Road, Oxford OX1 3TA, UK)

  • John Offer

    (The Scripps-Oxford Laboratory, University of Oxford, Mansfield Road, Oxford OX1 3QU, UK)

  • Johanna C. Scheinost

    (The Scripps-Oxford Laboratory, University of Oxford, Mansfield Road, Oxford OX1 3QU, UK)

  • Tomasz Borowski

    (Institute of Catalysis and Surface Chemistry, PAS University, Niezapominajek 830-239 Cracow, Poland)

  • Michael Sundstrom

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

  • Christopher J. Schofield

    (University of Oxford, Mansfield Road, Oxford OX1 3TA, UK)

  • Udo Oppermann

    (Structural Genomics Consortium, Botnar Research Center, University of Oxford, Oxford OX3 7LD, UK)

Abstract

Methylation of histone lysine residues can be reversed through the action of demethylases such as JMJD2A. Structures of JMJD2A bound to various methylated histone H3 peptides offer insight into the recognition mechanisms and specificity of histone demethylases.

Suggested Citation

  • Stanley S. Ng & Kathryn L. Kavanagh & Michael A. McDonough & Danica Butler & Ewa S. Pilka & Benoit M. R. Lienard & James E. Bray & Pavel Savitsky & Opher Gileadi & Frank von Delft & Nathan R. Rose & J, 2007. "Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity," Nature, Nature, vol. 448(7149), pages 87-91, July.
    • Handle: RePEc:nat:nature:v:448:y:2007:i:7149:d:10.1038_nature05971
    DOI: 10.1038/nature05971
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