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Issue 12, 2014
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Structural biology and chemistry of protein arginine methyltransferases

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Abstract

Protein arginine methyltransferases (PRMTs), an emerging target class in drug discovery, can methylate histones and other substrates, and can be divided into three subgroups, based on the methylation pattern of the reaction product (monomethylation, symmetrical or asymmetrical dimethylation). Here, we review the growing body of structural information characterizing this protein family, including structures in complex with substrate-competitive and allosteric inhibitors. We outline structural differences between type I, II and III enzymes and propose a model underlying class-specificity. We analyze the structural plasticity and diversity of the substrate, cofactor and allosteric binding sites, and propose that the conformational dynamics of PRMTs can be exploited towards the discovery of allosteric inhibitors that would antagonize conformationally active states.

Graphical abstract: Structural biology and chemistry of protein arginine methyltransferases

  • This article is part of the themed collection: Epigenetics
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Publication details

The article was received on 24 Jun 2014, accepted on 20 Aug 2014 and first published on 21 Aug 2014


Article type: Review Article
DOI: 10.1039/C4MD00269E
Citation: Med. Chem. Commun., 2014,5, 1779-1788
  • Open access: Creative Commons BY license
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    Structural biology and chemistry of protein arginine methyltransferases

    M. Schapira and R. Ferreira de Freitas, Med. Chem. Commun., 2014, 5, 1779
    DOI: 10.1039/C4MD00269E

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