Literature summary for 2.3.2.26 extracted from

Zhang, W.; Wu, K.; Sartori, M.; Kamadurai, H.; Ordureau, A.; Jiang, C.; Mercredi, P.; Murchie, R.; Hu, J.; Persaud, A.; Mukherjee, M.; Li, N.; Doye, A.; Walker, J.; Sheng, Y.; Hao, Z.; Li, Y.; Brown, K.; Lemichez, E.; Chen, J.; Tong, Y.; Harper, J.; Moffat, J.
System-wide modulation of HECT E3 ligases with selective ubiquitin variant probes (2016), Mol. Cell., 62, 121-136 .

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Application

Application	Comment	Organism
analysis	development of ubiquitin variants that inhibit or activate HECT E3 enzymes. Ubiquitin variant inhibitors block the E2-binding site, and activators occupy a ubiquitin-binding exosite. Ubiquitin variants reveal regulation mechanisms among NEDD4 subfamily HECTs and are useful for modulating therapeutically relevant targets of HECT E3s in cells and intestinal organoids. Ubiquitin variant activators bind to the N-lobe exosite and differentially modulate related HECT E3 ligases	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of ubiquitin variants in complex with the HECT domains of human E3 HECT ligases	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)