Selected article for: "CT peptide and pdz domain"
Author: Teoh, Kim-Tat; Siu, Yu-Lam; Chan, Wing-Lim; Schlüter, Marc A.; Liu, Chia-Jen; Peiris, J. S. Malik; Bruzzone, Roberto; Margolis, Benjamin; Nal, Béatrice
Title: The SARS Coronavirus E Protein Interacts with PALS1 and Alters Tight Junction Formation and Epithelial Morphogenesis
  • Document date: 2010_11_15
    • ID: ufw13pjx_57
    Snippet: As expected, both the myc-CRB3 and the HA-E (wt) proteins were pulled down by GST-PDZ in absence of peptide (Figure 4C, panels a and b, lane 3). By contrast, the CT peptide of E drastically inhibited the interaction of myc-CRB3, but not HA-E (wt), with PALS1 PDZ in a dose-dependent manner (Figure 4C, panels a and b, lanes 4–5). Conversely, the CRB3 CT peptide could abrogate the interaction of both myc-CRB3 and HA-E (wt) interaction with PALS1 P.....
    Document: As expected, both the myc-CRB3 and the HA-E (wt) proteins were pulled down by GST-PDZ in absence of peptide (Figure 4C, panels a and b, lane 3). By contrast, the CT peptide of E drastically inhibited the interaction of myc-CRB3, but not HA-E (wt), with PALS1 PDZ in a dose-dependent manner (Figure 4C, panels a and b, lanes 4–5). Conversely, the CRB3 CT peptide could abrogate the interaction of both myc-CRB3 and HA-E (wt) interaction with PALS1 PDZ (Figure 4C, panels a and b, lanes 6–7). These data indicate that the carboxy-terminal of E can compete out the interaction of CRB3 with the PDZ domain of PALS1 in vitro.

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