A. Stadler

The C-terminus of CFAP410 forms a tetrameric helical bundle that is essential for its localization to the basal body

This study determines the structure of CFAP410's C-terminal domain and shows that its tetrameric helical bundle is essential for basal body localization, explaining how the L224P mutation causes ciliopathies.

CFAP410 has a bimodular architecture with a conserved surface patch on its N-terminal LRR motif for binding interaction partners

This study reports the crystal structure of the N-terminal domain of CFAP410 and shows how mutations in this domain disrupt its structural stability and interaction with partners, leading to disease.