We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms.
Atomic-resolution monitoring of protein maturation in live human cells by NMR / Banci L; Barbieri L; Bertini I; Luchinat E; Secci E; Zhao Y; Aricescu AR. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - STAMPA. - 9:(2013), pp. 297-299. [10.1038/NCHEMBIO.1202]
Atomic-resolution monitoring of protein maturation in live human cells by NMR.
BANCI, LUCIA
;BARBIERI, LETIZIA;BERTINI, IVANO;LUCHINAT, ENRICO;SECCI, ERICA;
2013
Abstract
We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms.
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