Literature summary for 2.3.2.26 extracted from

Maspero, E.; Valentini, E.; Mari, S.; Cecatiello, V.; Soffientini, P.; Pasqualato, S.; Polo, S.
Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming (2013), Nat. Struct. Mol. Biol., 20, 696-701.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of ubiquitin-loaded human neural precursor cellexpressed developmentally downregulated protein, Nedd4, to 2.51 A resolution. The Nedd4-HECT domain-ubiquitin transitory intermediate provides a structural basis for the proposed sequential addition mechanism. The donor ubiquitin, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. Nedd4-family members are Lys63-specific enzymes whose catalysis is mediated by an essential C-terminal acidic residue	Homo sapiens

Crystallization (Comment)

Organism

structure of ubiquitin-loaded human neural precursor cellexpressed developmentally downregulated protein, Nedd4, to 2.51 A resolution. The Nedd4-HECT domain-ubiquitin transitory intermediate provides a structural basis for the proposed sequential addition mechanism. The donor ubiquitin, transferred from the E2, is bound to the Nedd4 C lobe with its C-terminal tail locked in an extended conformation, primed for catalysis. Nedd4-family members are Lys63-specific enzymes whose catalysis is mediated by an essential C-terminal acidic residue

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P46934	-	-

Synonyms

Synonyms	Comment	Organism
Nedd4	-	Homo sapiens

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Release 2023.1 (January 2023)