Homozygous Inactivating Mutation in NANOS3 in Two Sisters with Primary Ovarian Insufficiency

Figure 4

In silico analysis of amino acid interaction modification shows the different conformation conferred by the p.Glu120Lys substitution. Glutamic acid 120 (shown as E120) makes a hydrophobic interaction with lysine 96 (K96) and hydrogen bonds with both glycine 116 (G116) and threonine 124 (T124). The substitution to lysine 120 (K120) modifies structural points of contact establishing a new interaction with histidine 123 (His123) through aromatic stacking and abolishes the hydrophobic interaction with K96.