IndraLab

Statements

OTUD5 binds Ubiquitin. 6 / 6
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"Huang et al. reported the crystal structure of the pSer177 OTUD5–Ub complex."
37190070
sparser
"In the second method, after phosphorylation modification, the conformation of DUBs changes only after binding to the substrate, such as the phosphorylated DUBA bound to Ub, which alters its conformation instead of the phosphorylated DUBA [ xref ]."
36142702
sparser
"Huang et al. reported the crystal structure of the pSer177 OTUD5–Ub complex."
37190070
sparser
"The crystal structure of the Ub-aldehyde complex with phosphorylated OTUD5 reveals a remarkable interaction between the phosphorylated Ser177 of OTUD5 and the guanidinium moiety of Arg74 of the bound ubiquitin showing that the phosphorylation is essential for the DUB activity [ xref ]."
32512887
sparser
"In the crystal structure of OTUD5 bound with ubiquitin ( xref ), Asp256, Arg274, and Asn293 are located on the surface of the protein, and form no direct interactions with ubiquitin ( xref )."
33748114
sparser
"In the crystal structure of the Ser177-phosphorylated form of OTUD5 bound with ubiquitin ( xref ), the phosphate group has intramolecular interactions with other OTUD5 polar residues (including Arg272), and also has intermolecular interactions with the C-terminal tail of the bound ubiquitin, precisely orienting its C-terminus for catalysis."
33748114