Fig. 1: Ub4a binding to the distal Ub of Ub4 and Ub3 chains with four C-terminal residues, LRGG, deleted in the proximal Ub (ΔLRGG). | Nature Communications

Fig. 1: Ub4a binding to the distal Ub of Ub4 and Ub3 chains with four C-terminal residues, LRGG, deleted in the proximal Ub (ΔLRGG).

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

Fig. 1

Overlays of 1H-15N SOFAST-HMQC NMR spectra of the distal Ub of a [Ub]3-UbR72 free in solution (blue) and upon addition of Ub4a (red); b [Ub]2-UbR72 free in solution (blue) and upon addition of Ub4a (red); c wild-type Ub3 (blue) and [Ub]3-UbR72 (red) at the endpoint of titration with Ub4a; d wild-type Ub2 (blue) and [Ub]2-UbR72 (red) at the endpoint of titration with Ub4a. Note the similarities between the blue and red spectra in c and also 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. e Schematic representations of the amino acid composition of the cyclic peptide Ub4a.

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