Abstract
Correction to: The EMBO Journal (2008) 27, 1758–1766. doi:10.1038/emboj.2008.97
Since the publication of the above paper, the authors have noticed errors in Figure 4.
The correct figure is shown below.
Figure 1.
Etk activation through Y574 phosphorylation. (A) Dephosphorylated Y574 blocks substrate access to the active site. The residue, once phosphorylated, is likely to find an alternative conformation, such as binding to R614, therefore making the active site accessible to substrates. (B) The active site of P. furiosus MinD complexed with ADP (PDB code 1G3Q; Hayashi et al, 2001). (C) Modelled Etk C-terminal peptide (715–722, YNYYGYSY) is docked to the active site of the Etk–ADP complex structure, with the P-Y574 side chain interacting with R614. The magnesium cation, coloured green, is not present in the current Etk structure (due to the presence of EDTA in the crystallization buffer) and hence modelled from the same atom in MinD structure (PDB code 1G3R; Hayashi et al, 2001). Y718 of the peptide substrate is positioned to be phosphorylated. The Etk–peptide complex model is energy minimized. (D) The activation loop of insulin-like growth factor-1 receptor kinase (PDB code 1K3A; Favelyukis et al, 2001). The phosphorylation of Y1131, Y1135 and Y1136 stabilizes the activation loop far away from the active site (orange), which is now occupied by the ATP analogue (green) and the peptide substrate (magenta). When these three Tyr residues are dephosphorylated (PDB code 1IRK; Hubbard et al, 1994), the activation loop occupies the same location as the peptide substrate, inhibiting its kinase activity.
The updated e-mail address for the corresponding author is jia@queensu.ca
The authors apologize for any inconvenience caused.