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Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase
Abstract
Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene ( SOD1 ) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation Ala 4 to Val in exon 1 was the most frequent one; mutations were identified in exons 2, 4, and 5 but not in the active site region formed by exon 3. The 2.4 Å crystal structure of human SOD, along with two other SOD structures, established that all 12 observed FALS mutant sites alter conserved interactions critical to the β-barrel fold and dimer contact, rather than catalysis. Red cells from heterozygotes had less than 50 percent normal SOD activity, consistent with a structurally defective SOD dimer. Thus, defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of FALS.
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Metadata
- Authors
- Deng, H.-X., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W.-Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., Warner, C., Deng, G., Soriano, E., Smyth, C., Parge, H. E., Ahmed, A., Roses, A. D., Hallewell, R. A., Pericak-Vance, M. A., & Siddique, T.
- Venue
- Science
- Published
- 1993-08-20
- Volume
- 261
- Issue
- 5124
- Pages
- 1047-1051
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2166155593
- Cited by
- 1,477
- References
- 3
- FWCI
- 69.07
- Type
- journal article
- Language
- en
- Open access
- closed
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