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Structure 2014 Feb 04;222:337-44. doi: 10.1016/j.str.2013.12.004.
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Structure of the human FANCL RING-Ube2T complex reveals determinants of cognate E3-E2 selection.

Hodson C , Purkiss A , Miles JA , Walden H .

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.

PubMed ID: 24389026
PMC ID: PMC3979106
Article link: Structure
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: cbl fancd2 fancl rnf2 ubc ube2d1 ube2d3 ube2l3 ube2t

Article Images: [+] show captions
References [+] :
Afonine, A robust bulk-solvent correction and anisotropic scaling procedure. 2005, Pubmed