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Figure 2.
Figure 2. Comparison of Wild-Type and Analog-Specific c-Src
Crystal Structures(A) The crystal structure of c-Src-as1
superimposed on wild-type c-Src. c-Src-as1 is shown in gray, and
c-Src is in red. The rmsd for the overlay is 0.35 Å.(B)
The binding of the A*TP analog, N^6-(benzyl) ADP to the mutant
c-Src (T338G) kinase. The surface corresponding to the glycine
residue at the 338 position is colored red. The benzyl ring of
the A*TP analog projects into a pocket in the nucleotide binding
cleft. This pocket is made accessible by the c-Src (T338G) point
mutation. For clarity, the 11 residues that bind over the
nucleotide at the front of the nucleotide cleft are omitted from
the figure in order to more clearly show the surface at the back
of the nucleotide binding pocket where the 338 residue lies. The
omitted residues are c-Src 272–282.(C) The steric clash of the
wild-type c-Src threonine residue at the 338 position, shown in
red, with the N^6-(benzyl) ATP analog (blue). The gray surface
was built over the crystal structure of the mutant kinase
overlayed with the wild-type c-Src crystal structure, and the
surface was rendered over threonine 338 (red). The N^6-(benzyl)
ADP (blue) is superimposed on the AMP-PNP ligand (yellow).
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