Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection

Charlotte Hodson, Andrew Purkiss, Jennifer Anne Miles, Helen Walden (Lead / Corresponding author)

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    64 Citations (Scopus)
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    Abstract

    The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic E3-E2 interactions are well established. Nevertheless, the determinants of selective, specific E3-E2 recognition are not understood. There are ~40 E2s and ~600 E3s giving rise to a possible ~24,000 E3-E2 pairs. Using the Fanconi Anemia pathway exclusive E3-E2 pair, FANCL-Ube2T, we report the atomic structure of the FANCL RING-Ube2T complex, revealing a specific and extensive network of additional electrostatic and hydrophobic interactions. Furthermore, we show that these specific interactions are required for selection of Ube2T over other E2s by FANCL.
    Original languageEnglish
    Pages (from-to)337-344
    JournalStructure
    Volume22
    Issue number2
    Early online date2 Jan 2014
    DOIs
    Publication statusPublished - Feb 2014

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