Fig. 4: XL44 forms extensive hydrophobic interactions with hRpn13 Pru.
From: A structure-based designed small molecule depletes hRpn13Pru and a select group of KEN box proteins
a Overlay of the model (XL44, dark pink; hRpn13 Pru, black) and experimental (XL44, light pink; hRpn13 Pru, purple) structures with ubiquitin omitted. b, c Expanded view of XL44-bound hRpn13 showing close contacts between XL44 H10 and H18 and hRpn13 Leu33, Val38, Val85 b and Met31 c with distances (Å) included. Interactions consistent with detected NOEs are represented with black lines and those that do not support an R stereo-configuration at C12 are displayed with orange lines. d–f Comparative structural analysis of hRpn13 Pru bound with XL44 (pink, d), hRpn2 peptide (940–953, e) (light orange) or XL5 (orange, f) with similar interactions highlighted (black lines with distances (Å) included) for the XL44 methoxybenzamide and hRpn2 Pro944 and Pro945. Distinct interactions are highlighted for XL5 4-methylbenzamide. g, h Expanded view of extensive hydrophobic interactions between the XL44 central benzene g and indolin-2-one h rings with hRpn13 Pru residues. Colored as in Fig. 2a.
