Skip to main content
. 2025 Sep 24;14(9):e250444. doi: 10.1530/EC-25-0444

Table 2.

Local interaction profiles of conserved and cancer-associated MEP50 mutations. Change in folding free energy (ΔΔG, kcal/mol) for MEP50 mutants, as calculated by structural modeling. W59R and W152K affect conserved tryptophan residues critical for WD40 domain integrity, while A97T, E107K, and A303V correspond to somatic mutations found in endocrine cancers.

Mutation Energy Effect
W59R 5.66 Destabilizing
W152K 6.2 Destabilizing
A97T −1.06 Destabilizing
E107K 1.97 Destabilizing
A303V 1.57 Destabilizing