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Literature summary for 1.15.1.1 extracted from

  • DiDonato, M.; Craig, L.; Huff, M.E.; Thayer, M.M.; Cardoso, R.M.F.; Kassmann, C.J.; Lo, T.P.; Bruns, C.K.; Powers,E.T.; Kelly, J.W.; Getzoff, E.D; Tainer, J.A.
    ALS Mutants o human superoxide dismutase form fibrous aggregates via framework destabilization (2003), J. Mol. Biol., 332, 601-615.
    View publication on PubMed

Application

Application Comment Organism
medicine superoxide dismutase enzyme mutations causing familial amyotrophic lateral scerosis FALS cluster in protein regions influencing architectural integrity. FALS mutants H43R and A4V show reduced stability and drastically increased aggregation propensity, promoting the formation of filamentous aggregates. Free-cysteine-independent aggregation of FALS mutant enzyme is an intregral part of pathology Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type, beta-barrel mutant H43R, dimer interface mutant A4V Homo sapiens

Protein Variants

Protein Variants Comment Organism
A4V mutation causing familial amyotrophic lateral scerosis, 30% of wild-type activity, 1.06 atoms of copper and 1.43 atoms of zinc per subunit Homo sapiens
H43R mutation causing familial amyotrophic lateral scerosis, 59% of wild-type activity, 1.4 atoms of copper and 1.11 atoms of zinc per subunit Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
copper wild-type, 0.98 atoms per subunit, mutant H43R, 1.42, mutant A4V, 1.06 atoms per subunit Homo sapiens
Zinc wild-type, 1.08 atoms per subunit, mutant H43R, 1.11, mutant A4V, 1.43 atoms per subunit Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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patients with familial amyotrophic lateral scerosis FALS
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