Atomic-resolution monitoring of protein maturation in live human cells by NMR.
 

Atomic-resolution monitoring of protein maturation in live human cells by NMR.

Atomic-resolution monitoring of protein maturation in live human cells by NMR.

Nat Chem Biol. 2013 Mar 3;

Authors: Banci L, Barbieri L, Bertini I, Luchinat E, Secci E, Zhao Y, Aricescu AR

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. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment.


PMID: 23455544 [PubMed - as supplied by publisher]



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