What question did this study set out to answer?

This analysis aims to understand how RET gene mutations contribute to Hirschsprung's disease and MEN2A.

Systematic structure-based analysis of RET variants in MEN2A, Hirschsprung's disease, and their paradoxical co-occurrence

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Systematic analysis reveals structural impacts of RET mutations in Hirschsprung's disease and MEN2A, suggesting new therapies.

This analysis aims to understand how RET gene mutations contribute to Hirschsprung's disease and MEN2A.
Curated 77 RET extracellular positions linked to diseases.
Applied structure-based predictions of mutation effects on RET structure.
Analyzed mutation impacts on RET tertiary structure and protein interactions.
90% of HSCR-associated mutations disrupt intramolecular interactions stabilizing RET.
75% of MEN2A mutations lead to unpaired cysteines forming disulfide bonds between RET monomers.
Some mutations destabilize RET structure and promote both HSCR and MEN2A co-occurrence.

Bakhman et al. (2026) studied this question.

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