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 (Comment) | Organism |
---|---|
wild-type, beta-barrel mutant H43R, dimer interface mutant A4V | Homo sapiens |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
patients with familial amyotrophic lateral scerosis FALS | - |