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Ankyrin for methylated lysines

Nature Structural & Molecular Biology volume 15, pages 221–222 (2008)Cite this article

The ankyrin repeats of the G9a and GLP histone methyltransferases have now been shown to be binding modules for mono- and dimethyllysine histone H3 lysine 9 (H3K9), revealing a new function for an ankyrin repeat domain and showing that a polypeptide chain can both create and recognize the same histone mark.

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Figure 1: Structures of methyllysine binding domains in complex with their methyllysine-containing target peptides, showing the overall domain structure (above), a surface representation of the methyllysine binding pocket (middle) and a schematic representation of the aromatic cage (below).

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Authors and Affiliations

  1. Michael M. Brent and Ronen Marmorstein are at the Wistar Institute and the Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. marmor@wistar.org,

    Michael M Brent & Ronen Marmorstein

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  1. Michael M Brent
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  2. Ronen Marmorstein
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Brent, M., Marmorstein, R. Ankyrin for methylated lysines. Nat Struct Mol Biol 15, 221–222 (2008). https://doi.org/10.1038/nsmb0308-221

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