This study investigates the molecular effects of the disease-associated p.Met128Lys (M128K) mutation in human GLRX5, a mitochondrial protein involved in [2Fe-2S] cluster biogenesis. By combining structural and functional characterization, the study aims to determine whether M128K affects protein folding, Fe-S cluster binding, interaction with BOLA3, or cluster transfer to NFU1, providing molecular insights into its contribution to congenital sideroblastic anemia.
MOLECULAR IMPACT OF THE GLRX5 MET128LYS MUTATION IN HUMAN CONGENITAL SIDEROBLASTIC ANEMIA / Rosanna Cuccaro, Lucia Banci. - ELETTRONICO. - (2026), pp. 1-1. (Four Years of FeSImmChemNet: From Biochemistry to Immunology Seville ).
MOLECULAR IMPACT OF THE GLRX5 MET128LYS MUTATION IN HUMAN CONGENITAL SIDEROBLASTIC ANEMIA
Rosanna Cuccaro;Lucia Banci
2026
Abstract
This study investigates the molecular effects of the disease-associated p.Met128Lys (M128K) mutation in human GLRX5, a mitochondrial protein involved in [2Fe-2S] cluster biogenesis. By combining structural and functional characterization, the study aims to determine whether M128K affects protein folding, Fe-S cluster binding, interaction with BOLA3, or cluster transfer to NFU1, providing molecular insights into its contribution to congenital sideroblastic anemia.
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