Matches in SemOpenAlex for { <https://semopenalex.org/work/W2037607907> ?p ?o ?g. }
- W2037607907 abstract "Ubiquitination by HECT E3 enzymes regulates myriad processes, including tumor suppression, transcription, protein trafficking, and degradation. HECT E3s use a two-step mechanism to ligate ubiquitin to target proteins. The first step is guided by interactions between the catalytic HECT domain and the E2∼ubiquitin intermediate, which promote formation of a transient, thioester-bonded HECT∼ubiquitin intermediate. Here we report that the second step of ligation is mediated by a distinct catalytic architecture established by both the HECT E3 and its covalently linked ubiquitin. The structure of a chemically trapped proxy for an E3∼ubiquitin-substrate intermediate reveals three-way interactions between ubiquitin and the bilobal HECT domain orienting the E3∼ubiquitin thioester bond for ligation, and restricting the location of the substrate-binding domain to prioritize target lysines for ubiquitination. The data allow visualization of an E2-to-E3-to-substrate ubiquitin transfer cascade, and show how HECT-specific ubiquitin interactions driving multiple reactions are repurposed by a major E3 conformational change to promote ligation. DOI:http://dx.doi.org/10.7554/eLife.00828.001." @default.
- W2037607907 created "2016-06-24" @default.
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- W2037607907 date "2013-08-08" @default.
- W2037607907 modified "2023-10-05" @default.
- W2037607907 title "Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3" @default.
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- W2037607907 doi "https://doi.org/10.7554/elife.00828" @default.
- W2037607907 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3738095" @default.
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