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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)

  1. Ligand binding and aggregation of pathogenic SOD1. Wright GS, Antonyuk SV, Kershaw NM, Strange RW, Samar Hasnain S. Nat Commun 4 1758 (2013)
  2. Modulating protein-protein interactions with small molecules: the importance of binding hotspots. Thangudu RR, Bryant SH, Panchenko AR, Madej T. J Mol Biol 415 443-453 (2012)
  3. Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant. Ip P, Sharda PR, Cunningham A, Chakrabartty S, Pande V, Chakrabartty A. Protein Eng Des Sel 30 431-440 (2017)
  4. Parsing disease-relevant protein modifications from epiphenomena: perspective on the structural basis of SOD1-mediated ALS. Schmitt ND, Agar JN. J Mass Spectrom 52 480-491 (2017)
  5. Assessment of ligand binding at a site relevant to SOD1 oxidation and aggregation. Manjula R, Wright GSA, Strange RW, Padmanabhan B. FEBS Lett 592 1725-1737 (2018)
  6. Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis. Anzai I, Toichi K, Tokuda E, Mukaiyama A, Akiyama S, Furukawa Y. Front Mol Biosci 3 40 (2016)
  7. Pentachlorophenol molecule design with lower bioconcentration through 3D-QSAR associated with molecule docking. Wang X, Chu Z, Yang J, Li Y. Environ Sci Pollut Res Int 24 25114-25125 (2017)
  8. Lipid-associated aggregate formation of superoxide dismutase-1 is initiated by membrane-targeting loops. Chng CP, Strange RW. Proteins 82 3194-3209 (2014)
  9. A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformers. Healy EF. PLoS One 12 e0177284 (2017)
  10. The role of hydration effects in 5-fluorouridine binding to SOD1: insight from a new 3D-RISM-KH based protocol for including structural water in docking simulations. Hinge VK, Blinov N, Roy D, Wishart DS, Kovalenko A. J Comput Aided Mol Des 33 913-926 (2019)
  11. Cloning and high-level expression of monomeric human superoxide dismutase 1 (SOD1) and its interaction with pyrimidine analogs. LeVatte M, Lipfert M, Roy D, Kovalenko A, Wishart DS. PLoS One 16 e0247684 (2021)
  12. Tryptophan residues in TDP-43 and SOD1 modulate the cross-seeding and toxicity of SOD1. Pokrishevsky E, DuVal MG, McAlary L, Louadi S, Pozzi S, Roman A, Plotkin SS, Dijkstra A, Julien JP, Allison WT, Cashman NR. J Biol Chem 300 107207 (2024)


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