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Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.

Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ
Arch Biochem Biophys 492 40-7 (2009)
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Cited: 49 times
EuropePMC logo PMID: 19800308

Abstract

Amyotrophic lateral sclerosis (ALS) is a fatal, progressive neurodegenerative disease characterized by the destruction of motor neurons in the spinal cord and brain. A subset of ALS cases are linked to dominant mutations in copper-zinc superoxide dismutase (SOD1). The pathogenic SOD1 variants A4V and G93A have been the foci of multiple studies aimed at understanding the molecular basis for SOD1-linked ALS. The A4V variant is responsible for the majority of familial ALS cases in North America, causing rapidly progressing paralysis once symptoms begin and the G93A SOD1 variant is overexpressed in often studied murine models of the disease. Here we report the three-dimensional structures of metal-free A4V and of metal-bound and metal-free G93A SOD1. In the metal-free structures, the metal-binding loop elements are observed to be severely disordered, suggesting that these variants may share mechanisms of aggregation proposed previously for other pathogenic SOD1 proteins.

Reviews - 3gzo mentioned but not cited (1)

  1. Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants. Huai J, Zhang Z. Front Neurol 10 527 (2019)

Articles - 3gzo mentioned but not cited (6)

  1. Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ. Arch Biochem Biophys 492 40-47 (2009)
  2. Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs). Boyd SD, Ullrich MS, Calvo JS, Behnia F, Meloni G, Winkler DD. Molecules 25 E1086 (2020)
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Reviews citing this publication (3)

  1. Superoxide dismutases and superoxide reductases. Sheng Y, Abreu IA, Cabelli DE, Maroney MJ, Miller AF, Teixeira M, Valentine JS. Chem Rev 114 3854-3918 (2014)
  2. An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis. Rotunno MS, Bosco DA. Front Cell Neurosci 7 253 (2013)
  3. Is amyotrophic lateral sclerosis/frontotemporal dementia an autophagy disease? Deng Z, Sheehan P, Chen S, Yue Z. Mol Neurodegener 12 90 (2017)

Articles citing this publication (39)

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