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Figure 1.
Crystallographic snapshot of the trans-phosphorylation
reaction at Y769, a major phosphorylation site in FGFR2K. (A)
The substrate-acting kinase (in yellow) interacts with both N-
and C-lobe of the enzyme-acting kinase (in green) during the
trans-phosphorylation on Y769. (B) The tyrosine of the peptide
substrate in the kinase-peptide structure (in blue) occupies a
similar position as the Y769 in the substrate-acting kinase. (C)
The trans-phosphorylation reaction on Y769 phosphorylation site.
The near parallel arrangement of the αI helix from the
substrate-acting kinase and the αG helix from the enzyme-acting
kinase is denoted by the two arrows. The extra ordered residues
at the C-tail of the trans-phosphorylating kinases structure
compared with the kinase-peptide structure are highlighted in
magenta. (D) The interaction between the C-lobe of the
substrate-acting kinase and the N-lobe of the enzyme-acting
kinase. Selected residues are show in stick diagrams. Atom
colorings are as follows: red, oxygens; blue, nitrogens; yellow,
phosphorus; carbons are colored according to the kinase molecule
to which they belong. Hydrogen bonds are shown as black dashed
lines. The ATP analogue (in cyan) is shown in stick
representation, and its molecular surface is also shown as a
solid semitransparent surface. Mg^2+ ions are in pink.
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