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. (2nd EuChemS Chemical Biology School on “Biophysical Approaches in Chemical Biology and Drug Discovery” ).
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.
| File | Dimensione | Formato | |
|---|---|---|---|
|
Cuccaro_rosanna.docx
accesso aperto
Tipologia:
Pdf editoriale (Version of record)
Licenza:
Open Access
Dimensione
43.98 kB
Formato
Microsoft Word XML
|
43.98 kB | Microsoft Word XML |
I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
