1H, 13C and 15N assignment of the human mitochondrial paramagnetic iron-sulfur protein CISD3

CISD3 is a mitochondrial protein that contains two [2Fe-2S] clusters. This protein is overexpressed in some types of cancer, so it has emerged as a potential drug target. A detailed characterization of this protein is crucial to understand how CISD3 is involved in these physiopathologies. In this study, isotopically labeled human CISD3 was expressed in Escherichia coli. A set of double and triple resonance experiments performed with standard parameters/datasets provided the assignment of 40% of the HN resonances, 47% of C alpha, and 46% of C & PRIME; resonances. Tailored paramagnetic HSQC, CON and CACO experiments extended up to 59% for HN, 70% for C alpha and 69% for C & PRIME;. The H-1, C-13 and N-15 NMR chemical shift assignment of human CISD3 is reported here.

Automated summary

CISD3 is a mitochondrial protein with two [2Fe-2S] clusters. It is overexpressed in certain cancers, making it a potential target for drug therapy. This study successfully characterized human CISD3 using isotopically labeled samples and NMR techniques, providing valuable information for understanding its role in cancer development.