(A) Schematic of YAP protein structure, overlaid on to AlphaFold prediction expected position error of folded domains. Darker colours show a higher confidence in predicted relationship between residues. In general, a high level of predicted error persists throughout the various YAP domains, with just WW and CC domains exhibiting high levels of structural predictability. (B) Schematic of TAZ, as in (A), highlighting the high levels of intrinsic disorder that exists outside WW and CC domains. (C) Schematic of TEAD4, as in (A), with a higher degree of confidence in protein structure prediction observed throughout, as compared with YAP and TAZ proteins, suggesting a higher degree of structural order in TEAD4. Abbreviations: CC, coiled-coil domain; PDZ, PDZ-binding domain; TEA, TEA domain; YBD, YAP-binding domain.