IndraLab

Statements

UBD binds OTULIN. 6 / 7
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reach
"OTULIN binding to di-ubiquitin is characterized by a substrate-assisted catalysis step, in which the catalytic triad is only activated upon tight substrate binding (Keusekotten et al., 2013)."
34869597
sparser
"OTULIN binds Met1-linked diubiquitin with a K D of 150 nM, 100-fold higher affinity than Lys63-linked diubiquitin [ xref ]."
27913667
sparser
"Nevertheless, simply mutating the catalytic Cys in DUBs to Ala or Ser, as used for A20 xref , xref , is problematic, as this potentially converts the DUB domain to a high‐affinity UBD; OTULIN C129A binds Met1‐diubiquitin with nanomolar affinity, and interferes with NF‐κB signalling in artificial ways xref ."
26503766
sparser
"The structure of OTULIN bound to Met1-linked diubiquitin revealed extensive contacts between both distal and proximal ubiquitin moieties ( xref )."
27913667
sparser
"Indeed, OTULIN C129A binds Met1‐linked diubiquitin with 150 n m affinity, a 100‐fold greater affinity compared to topologically similar Lys63‐linked diubiquitin."
26503766
sparser
"OTULIN binding to di-ubiquitin is characterized by a substrate-assisted catalysis step, in which the catalytic triad is only activated upon tight substrate binding ( xref )."
34869597