Article
Extended Data Fig. 4 | Structural features of the SKP1/FBXL17-BTB
complex. a, Elution profile of the SKP1/FBXL17-BTB(KEAP1F64A) complex by
size exclusion chromatography detecting A 280. 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 (grey) 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.