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• W2000945872 abstract "Prp19 is an essential splicing factor and a member of the U-box family of E3 ubiquitin ligases. Prp19 forms a tetramer via a central coiled-coil domain. Here, we show the U-box domain of Prp19 exists as a dimer within the context of the Prp19 tetramer. A high-resolution structure of the homodimeric state of the Prp19 U-box was determined by X-ray crystallography. Mutation of the U-box dimer interface abrogates U-box dimer formation and is lethal in vivo. The structure of the U-box dimer enables construction of a complete model of Prp19 providing insights into how the tetrameric protein functions as an E3 ligase. Finally, comparison of the Prp19 U-box homodimer with the heterodimeric complex of BRCA1/BARD1 RING-finger domains uncovers a common architecture for a family of oligomeric U-box and RING-finger E3 ubiquitin ligases, which has mechanistic implications for E3 ligase-mediated polyubiquitination and E4 polyubiquitin ligases." @default.
• W2000945872 created "2016-06-24" @default.
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• W2000945872 date "2005-12-08" @default.
• W2000945872 modified "2023-10-10" @default.
• W2000945872 title "The Prp19 U-box Crystal Structure Suggests a Common Dimeric Architecture for a Class of Oligomeric E3 Ubiquitin Ligases^," @default.
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• W2000945872 doi "https://doi.org/10.1021/bi051787e" @default.
• W2000945872 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2570371" @default.
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