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Structural discovery of small molecule binding sites in Cu-Zn human superoxide dismutase familial amyotrophic lateral sclerosis mutants provides insights for lead optimization.

Antonyuk S, Strange RW, Hasnain SS
J Med Chem 53 1402-6 (2010)
Related entries: 2wyt, 2wyz, 2wz0, 2wz6

Cited: 16 times
EuropePMC logo PMID: 20067275

Abstract

Dominant inheritance of point mutations in CuZn superoxide dismutase (SOD1) is the best characterized subset of familial amyotrophic lateral sclerosis (FALS) and accounts for some 20% of the known familial cases. We report the discovery and visualization via cocrystallography of two ligand-binding pockets in human SOD1 and its pathogenic mutants that have opened up the real possibility of undertaking lead compound discovery using a fragment-based approach for therapeutic purposes for SOD1 associated motor neuron disease.

Reviews - 2wz5 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)


Reviews citing this publication (3)

  1. Unmet challenges of structural genomics. Chruszcz M, Domagalski M, Osinski T, Wlodawer A, Minor W. Curr Opin Struct Biol 20 587-597 (2010)
  2. Protein aggregation and therapeutic strategies in SOD1- and TDP-43- linked ALS. Tsekrekou M, Giannakou M, Papanikolopoulou K, Skretas G. Front Mol Biosci 11 1383453 (2024)
  3. Small molecules targeting different cellular pathologies for the treatment of amyotrophic lateral sclerosis. Elmansy MF, Reidl CT, Rahaman M, Özdinler PH, Silverman RB. Med Res Rev 43 2260-2302 (2023)

Articles citing this publication (12)



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