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Figure 3.
FIGURE 3. Structural insights of the SP600125-binding site.
A, detailed view of the structure of T686A-SP600125 complex,
showing SP600125 bound in the ATP-binding site. The residues
that interact with SP600125 are depicted as sticks. The 2F[o] -
F[c] map around SP600125 is shown, contoured at 1.5  . B,
surface representation (stereo view) of the inhibitor-binding
site in Mps1 and JNK1 (PDB ID 1UKI [PDB]
) with SP600125 shown in yellow. Important differences in the
composition and orientation of key residues
(Mps1^Lys-553/JNK1^Lys-55, Mps1^Cys-604/JNK1^Leu-110,
Mps1^Tyr-591/JNK1^Ile-106, Mps1^Tyr-568, Mps1^Glu-571,
JNK1^Glu-73, JNK1^Met-77, Mps1^Met-602/JNK1^Met-108, and
Mps1^Ile-663/JNK1^Leu-168) can be exploited for the rational
design of Mps1-specific inhibitors. C, surface representation of
the SP600125-binding site in human Mps1. A molecule of PEG from
the crystallization solution is bound in a secondary pocket next
to the catalytic Lys-553.
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