Fig. 2: Crystal structure of ASB7-Elongin B/C bound to the LZTS1-degron.
From: Molecular insights into degron recognition by CRL5ASB7 ubiquitin ligase
a Overall structure of ASB7-Elongin B/C bound to the LZTS1-degron peptide. ANK repeats, SOCS box, Elongin B and Elongin C are colored in pale green, lime green, light bule, and light pink, respectively. LZTS1-degron is shown in yellow. b Electrostatic potential surface of ASB7 bound to LZTS1-degron. Red, negative; Blue, positive. The helix-binding groove is ~30 Å long and ~9 Å wide. c Sequence alignment of ASB7 substrate degrons. The secondary structure and residues involved in site 1, site 2, and site 3 are indicated. d The α-helical LZTS1-degron is characterized three sites. Site 1, comprising five residues (yellow), is buried at the hydrophobic bottom of the binding groove. Site 2, comprising five residues (green), resides at the solvent-exposed surface on one side of the positively charged groove. Site 3 (cyan) docks on the other side of the negatively charged groove. e Cross-section view of the three different sites.
