Literature summary for 2.3.2.31 extracted from

Lechtenberg, B.C.; Rajput, A.; Sanishvili, R.; Dobaczewska, M.K.; Ware, C.F.; Mace, P.D.; Riedl, S.J.
Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation (2016), Nature, 529, 546-550 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the fully active HOIP-RBR in its transfer complex with an E2-ubiquitin conjugate. HOIP-RBR binds the E2-ubiquitin conjugate in an elongated fashion, with the E2 and E3 catalytic centers aligned for ubiquitin transfer, which structurally both requires and enables a HECT-like mechanism. Three distinct helix-IBR-fold motifs form ubiquitin-binding regions that engage the activated ubiquitin of the E2-ubiquitin conjugate as well as an additional regulatory ubiquitin molecule	Homo sapiens

Crystallization (Comment)

Organism

structure of the fully active HOIP-RBR in its transfer complex with an E2-ubiquitin conjugate. HOIP-RBR binds the E2-ubiquitin conjugate in an elongated fashion, with the E2 and E3 catalytic centers aligned for ubiquitin transfer, which structurally both requires and enables a HECT-like mechanism. Three distinct helix-IBR-fold motifs form ubiquitin-binding regions that engage the activated ubiquitin of the E2-ubiquitin conjugate as well as an additional regulatory ubiquitin molecule

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96EP0	-	-

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Release 2023.1 (January 2023)