On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson disease - A combined computational and in vitro study (Articolo in rivista)

Type
Label
  • On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson disease - A combined computational and in vitro study (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Alternative label
  • Herrera, FE; Zucchelli, S; Jezierska, A; Lavina, ZS; Gustincich, S; Carloni, P (2007)
    On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson disease - A combined computational and in vitro study
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Herrera, FE; Zucchelli, S; Jezierska, A; Lavina, ZS; Gustincich, S; Carloni, P (literal)
Pagina inizio
  • 24905 (literal)
Pagina fine
  • 24914 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 282 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • INFM, DEMOCRITOS, Int Sch Adv Studies, I-34014 Trieste, Italy; Italian Inst Technol, SISSA Unit, I-34014 Trieste, Italy; Giovanno Armenise Garvard Fdn Lab, I-34012 Trieste, Italy (literal)
Titolo
  • On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson disease - A combined computational and in vitro study (literal)
Abstract
  • Mutations in the DJ-1 protein are present in patients suffering from familial Parkinson disease. Here we use computational methods and biological assays to investigate the relationship between DJ-1 missense mutations and the protein oligomeric state. Molecular dynamics calculations suggest that: (i) the structure of DJ-1 wild type (WT) in aqueous solution, in both oxidized and reduced forms, is similar to the crystal structure of the reduced form; (ii) the Parkinson disease-causing M26I variant is structurally similar to the WT, consistent with the experimental evidence showing the protein is a dimer as WT; (iii) R98Q is structurally similar to the WT, consistent with the fact that this is a physiological variant; and (iv) the L166P monomer rapidly evolves toward a conformation significantly different from WT, suggesting a change in its ability to oligomerize. Our combined computational and experimental approach is next used to identify a mutant (R28A) that, in contrast to L166P, destabilizes the dimer subunit-subunit interface without significantly changing secondary structure elements. (literal)
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