IndraLab

Statements



sparser
"We superimposed the crystal structures of USP46 in a non-covalent complex with WDR20 and WDR48 together with the covalent USP46ubiquitin complex."

sparser
"The USP46-bound ubiquitin is closer, however, sheltered adjacent to the concave inner face of the WDR48 ancillary domain."

sparser
"Binding of WDR20 to the UAF1-USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub-bound USP46."

reach
"Binding of WDR20 to the UAF1 and USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub bound USP46."

sparser
"Furthermore, difference density indicating the missing domain clearly extended from our extant WDR48 C terminus, encircling the USP46-bound ubiquitin and approaching the thumb subdomain of USP46 over [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Reminiscent of the Ub bound UAF1 and USP46 complex, the UAF1-USP12 structure features an L shaped architecture, in which the elongated UAF1 protein packs perpendicularly against the DUB enzyme (XREF_FIG and XREF_FIG)."

sparser
"Stabilization of a malleable apo USP46 to favor an active conformation would shift the equilibrium of association and promote productive interaction between ubiquitin and USP46."

sparser
"UAF1 activation of USP12 requires structural fine-tuning at the ubiquitin-binding site, while WDR20 directly regulates the catalytic center of the enzyme remotely, transforming USP12 into a compact structure similar to USP46-Ub [ xref ]."

sparser
"Jianping Yin et al determined the 1.9A ° resolution structure of a resolution structure of a covalently attached USP46 25–366 ubiquitin complex."

sparser
"The substrate is cradled between the fingers and the inner palm/thumb regions. xref Moreover, a Zintegrated by 4 conserved Cys residues stabilizes the USP46 subdomain of the tip of the fingers, and the active-site adopts a catalytically favorable conformation. xref The USP46:ubiquitin interface buries 1,825A ° 2 of surface area on each protein."

sparser
"As shown in Fig. xref , purified GST-USP46 interacted with the NRAS Q61R and NRAS Q61K mutant more strongly than NRAS WT and Q61L. We also modeled the structure of ubiquitinated NRAS in complex with USP46 using protein-protein docking (Schrödinger, LLC, New York, NY, 2023) based on the USP46-UB complex structure (PDB ID: 5CVM) and NRAS Q61K (PDB ID: 8VM2)."