Fig. 4: USP36 differentially interacts with the ubiquitin and Fubi C termini.
From: Molecular basis for ubiquitin/Fubi cross-reactivity in USP16 and USP36
a, Crystal structure of the USP36 catalytic ___domain (green) bound to the ubiquitin-PA probe (wheat). b, Crystal structure of the USP36 catalytic ___domain (blue) bound to the Fubi-PA probe (lilac). c, Superimposition of cartoon representations shown in a and b. USP subdomains and the α5 helix are labeled. Arrows indicate differences between Fubi- and ubiquitin-bound complexes. d, Depiction of Fubi and ubiquitin C-terminal sequences. e–g, Close-up view of the area shown in d where the C-terminal tail of ubiquitin (e) or Fubi (f) is guided to the catalytic center. A superposition is shown in g. Residues of USP36, Fubi and ubiquitin are labeled in colors according to the structure from which they are shown. Different orientations of residues in the USP36 blocking loop 1 after engagement of Fubi or ubiquitin are highlighted with black arrows.
