The PALB2 C-terminal WD40-type β-propeller domain is known to promote interaction with BRCA2, and its structure has demonstrated that deleting only the last four residues (the consequence of the PALB2 Y1183X cancer-associated nonsense mutation) is sufficient to disrupt the proper folding of the domain and render the protein unstable5,18,19. This evidence concerns the gene PALB2 and cancer.