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- W1569259946 abstract "PML protein is mainly present inside the nucleus in the form of PML nuclear bodies (PML-NB) and serves as anchoring point for various sumoylated transcription factors and regulators. It mediates activities, such as transcriptional regulation, antiviral defense, DNA replication, DNA repair, telomere lengthening, chromatin organization, cell cycle control, senescence, apoptosis, and tumor suppression. PML-NB is associated with acute promyelocytic leukemia (APL). All known isoforms of PML have conserved N-terminal RBCC region comprised of a RING finger domain followed by two B-boxes and coiled-coil region. The RING domain has been shown to possess SUMO E3 ligase activity and the B1-box can be poly-sumoylated. Both the RING domain and the B1-box are zinc finger proteins. Surprisingly, only the structure of the RING domain was determined in 1995 and no information on the structure of other part of the molecule is known. Here we will present the solution NMR structures and dynamics of the RING domain and the B1 box, as well as their interactions with Ubc9, SUMO and SUMO substrates. Grant Funding Source: Supported by a Grants NSC 101-2311-B-001-025 from The National Science Council" @default.
- W1569259946 created "2016-06-24" @default.
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- W1569259946 date "2014-04-01" @default.
- W1569259946 modified "2023-10-18" @default.
- W1569259946 title "Structures, dynamics, and interactions with UBC9 of the RING and B1‐box domains of promyelocytic leukemia protein (938.1)" @default.
- W1569259946 doi "https://doi.org/10.1096/fasebj.28.1_supplement.938.1" @default.
- W1569259946 hasPublicationYear "2014" @default.
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