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Figure 2.
Structural basis for the trans-phosphorylation on Y769 of
FGFR2K. (A) Detailed view of the interactions between the
substrate-acting kinase and the enzyme-acting kinase in the
vicinity of active site. (B) In the kinase-peptide structure,
the peptide substrate makes limited contacts with the enzyme.
(C) Detailed view of the hydrophobic interactions between the
L770 (P+1) and L772 (P+3) residues of the substrate-acting
kinase and the residues from the A-loop and the αG and αEF
helices of the enzyme-acting kinase. (D) Detailed view of the
interaction between the C-lobe of the substrate-acting kinase
and the nucleotide-binding loop of the enzyme-acting kinase.
Yellow, substrate-acting kinase; green, enzyme-acting kinase;
blue, kinase in the kinase-peptide structure; wheat, peptide
substrate. Atom colorings are as in Fig. 1. Hydrogen bonds, the
ATP analogue and Mg^2+ ions are rendered as in Fig. 1.
Hydrophobic interactions are rendered as solid semitransparent
surfaces.
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