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Structural modeling results of the wild-type Wnt family member 10A (WNT10A) protein and the p.Arg125Lys-mutated WNT10A protein. (A) There was a hydrogen bond between p.Arg125 and p.Glu340 in the wild-type WNT10A protein. (B) The original hydrogen bond vanished in the p.Arg125Lys-mutated WNT10A protein, and a new hydrogen bond between p.125Lys and p.Leu352 arose. The changes may lead to instability of the structure and affect the affinity to the receptor of WNT10A.
