: 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 Cα, and 46% of C' resonances. Tailored paramagnetic HSQC, CON and CACO experiments extended up to 59% for HN, 70% for Cα and 69% for C'. The 1H, 13C and 15N NMR chemical shift assignment of human CISD3 is reported here.
1H, 13C and 15N assignment of the human mitochondrial paramagnetic iron-sulfur protein CISD3 / Silva, José Malanho; Grifagni, Deborah; Cantini, Francesca; Piccioli, Mario. - In: BIOMOLECULAR NMR ASSIGNMENTS. - ISSN 1874-2718. - ELETTRONICO. - -:(2022), pp. 0-0. [10.1007/s12104-022-10113-3]
1H, 13C and 15N assignment of the human mitochondrial paramagnetic iron-sulfur protein CISD3
Grifagni, Deborah;Cantini, Francesca;Piccioli, Mario
2022
Abstract
: 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 Cα, and 46% of C' resonances. Tailored paramagnetic HSQC, CON and CACO experiments extended up to 59% for HN, 70% for Cα and 69% for C'. The 1H, 13C and 15N NMR chemical shift assignment of human CISD3 is reported here.File | Dimensione | Formato | |
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