Fig. 2: Ub4a binding to the distal Ub of Ub4 and Ub3 chains with two C-terminal residues, G75 and G76, deleted in the proximal Ub (ΔGG). | Nature Communications

Fig. 2: Ub4a binding to the distal Ub of Ub4 and Ub3 chains with two C-terminal residues, G75 and G76, deleted in the proximal Ub (ΔGG).

From: Mechanism of selective recognition of Lys48-linked polyubiquitin by macrocyclic peptide inhibitors of proteasomal degradation

Fig. 2

Overlays of 1H-15N NMR spectra of the distal Ub of a [Ub]3-UbR74 free in solution (blue) and upon addition of Ub4a (red); b [Ub]2-UbR74 free in solution (blue) and upon addition of Ub4a (red); c wild-type Ub4 (blue) and [Ub]3-UbR74 (red) at the endpoint of titration with Ub4a; d wild-type Ub3 (blue) and [Ub]2-UbR74 (red) at the endpoint of titration with Ub4a. Note the similarities between the blue and red spectra in c and in d. Insets in a and b show Ub structure with perturbed residues colored blue and hydrophobic patch residues shown as spheres. The cartoon drawings below c and d illustrate the peptide binding arrangement deduced from the NMR data. The peptide:polyUb molar ratio was 1.5:1.

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