IndraLab

Statements

sparser
"It is known that Val328 and Phe332 of AMSH-LP interact with ubiquitin Ile44, but structural comparison shows that the equivalent positions in Rpn11 (Val83 and Phe87) are oriented in an opposite direction from AMSH-LP ( xref B)."
33498168
sparser
"Cys282 is next to the active site, and in fact it makes a van der Waals contact with Leu73 of the distal ubiquitin in the structure of AMSH-LP DUB domain bound to Lys63-linked ubiquitin dimer. xref In the disulfide orientation, however, as seen in the model of AMSH244 bound to Lys63-linked diubiquitin (please see below), the contact is lost."
21888914
sparser
"Interestingly, in the structure of AMSH-LP DUB domain bound to Lys63-linked ubiquitin dimer, the corresponding residue pair is still seen in a similar position as the substrate-free form, xref suggesting that these residues close the active site during catalysis as well, perhaps to help position the scissile peptide bond or stabilize the transition state or both."
21888914
sparser
"The Oγ atom of AMSH’s Ser346 is pointing away from Glu64 of the proximal ubiquitin ( xref ), contrary to the equivalent residue in both free and ubiquitin-bound AMSH-LP, which are at distances of 2.4Å and 2.6Å from proximal ubiquitin’s Glu64, respectively."
21888914
sparser
"The structural basis for this recognition was elucidated with the homologous protein, AMSH-LP, bound to Lys63-linked dimer of ubiquitin ( xref )."
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