Journal
STRUCTURE
Volume 22, Issue 2, Pages 337-344Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.12.004
Keywords
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Funding
- Cancer Research UK
- Medical Research Council
- European Molecular Biology Organization Young Investigator Award
- MRC [MC_UU_12016/12] Funding Source: UKRI
- Cancer Research UK [17739] Funding Source: researchfish
- Medical Research Council [MC_UU_12016/12] Funding Source: researchfish
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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 similar to 40 E2s and similar to 600 E3s giving rise to a possible similar to 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.
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