IndraLab
Statements
sparser
"The crystal structure of the catalytic domain of the phosphorylated DUBA (p-DUBA) conjugated to ubiquitin-aldehyde revealed that the interactions between the phosphate group and the two positively charged residues, R272 and K273, in the α6 helix lead to the enclosure of the C-terminal tail of ubiquitin ( xref ). xref NMR studies show that phosphorylation induces minimal structural changes in the apo state of DUBA, xref raising the question of whether modulation of conformational dynamics plays a role in DUBA activation."
sparser
"The phosphorylated DUBA displays essentially the same predicted secondary structure, which is in good agreement with the crystal structures of both non-phosphorylated DUBA in free form (PDB ID: 3PFY) and phosphorylated DUBA covalently linked to ubiquitin aldehyde (PDB ID: 3TMP)."
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 ]."