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Article

The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.

Journal of molecular biology - 12 Jan 2007

Hörnberg Andreas, Logan Derek T, Marklund Stefan L, Oliveberg Mikael

Abstract excerpt

The gain of neurotoxic function in amyotrophic lateral sclerosis (ALS) has been linked to misfolding of the homodimeric enzyme Cu/Zn superoxide dismutase (SOD). Here, we present the crystal structure of fully cysteine-depleted human SOD (SOD(CallA)), representing a reduced, marginally stable intermediate on the folding pathway in vivo that has also been implicated as neurotoxic precursor state. A hallmark of this...

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PMID: 17070542
DOI: 10.1016/j.jmb.2006.09.048

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