Fig. 4: Structural analyses. | Nature Communications

Fig. 4: Structural analyses.

From: Wnt/β-catenin activation by mutually exclusive FBXW11 and CTNNB1 hotspot mutations drives salivary basal cell adenoma

Fig. 4

a Location of the recurrently mutated sites in β-catenin (I35) and FBXW11 (F517) in the FBXW11-SKP1 complex with a β-catenin peptide phosphorylated on S33 and S37 (PDB ID 6WNX). Relevant residues contributing to the intermolecular binding network stabilising the complex are indicated with their lateral chains. b Root mean square fluctuation (RMSF) plot showing the effects of the p.F517S substitution on the conformation of the region of the FBXW11 WDR domain involved in β-catenin binding. The residues at the two highest peaks of RMSF changes are indicated. The F-to-S substitution at position 517 increases the mobility of R468 and a small amino acid stretch adjacent to Y265, which are key residues in the interaction with β-catenin. Source data are provided as a Source Data file.

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