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  NEDD8 and ubiquitin ligation by cullin-RING E3 ligases

Baek, K., Scott, D. C., & Schulman, B. A. (2021). NEDD8 and ubiquitin ligation by cullin-RING E3 ligases. Current Opinion in Structural Biology, 67, 101-109. doi:10.1016/j.sbi.2020.10.007.

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Baek_2020_Curr_Opin_Struct_Biol.pdf (Publisher version), 3MB
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Baek, Kheewong1, Author              
Scott, Daniel C2, Author
Schulman, Brenda A.1, Author              
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1Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466699              
2external, ou_persistent22              

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 Abstract: RING E3s comprise the largest family of ubiquitin (UB) and ubiquitin-like protein (UBL) ligases. RING E3s typically promote UB or UBL transfer from the active site of an associated E2 enzyme to a distally-recruited substrate. Many RING E3s – including the cullin-RING ligase family – are multifunctional, interacting with various E2s (or other E3s) to target distinct proteins, transfer different UBLs, or to initially modify substrates with UB or subsequently elongate UB chains. Here we consider recent structures of cullin-RING ligases, and their partner E2 enzymes, representing ligation reactions. The studies collectively reveal multimodal mechanisms – interactions between ancillary E2 or E3 domains, post-translational modifications, or auxiliary binding partners – directing cullin-RING E3-E2 enzyme active sites to modify their specific targets.

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 Dates: 2021
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.sbi.2020.10.007
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Title: Current Opinion in Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 67 Sequence Number: - Start / End Page: 101 - 109 Identifier: ISBN: 0959-440X