Extended Data Figure 4: Structural features of the SKP1/FBXL17-BTB complex.
a. Elution profile of the SKP1/FBXL17-BTB(KEAP1F64A) complex by size exclusion chromatography detecting A280. Control proteins with known MW are shown on top. This experiment was performed three times. b. FBXL17 binds to SKP1 via its F-box domain, in a manner highly similar to the LRR-domain containing F-box proteins SKP2 and FBXL3 20,21. The structures of SKP1-FBXL17, SKP1-SKP2, and SKP1-FBXL3 were aligned via SKP1. FBXL17 is shown in orange, SKP2 in magenta, and FBXL3 in yellow. c. FBXL17 uses conserved residues in its F-box to bind SKP1. The highlighted residues in FBXL17 (orange) that bind SKP1 (gray) were adopted from ref. 21. d. The substrate binding LRR domain of FBXL17 is longer and more curved than the LRR domains of SKP2 or FBXL3. Complexes were aligned via SKP1 (FBXL17, orange; SKP2, magenta; FBXL3, yellow). e. Structural models of BTB-FBXL17 complexes, using BTB domains that are similar in shape, but distinct in sequence. All complexes between FBXL17 and these confirmed substrates 2 can be formed without steric clashes. f. SKP1 and Elongin C, which also adopt BTB folds, cannot be bound to FBXL17, due to steric clashes shown in the insets.