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Figure 4.
FIG. 4. The structure and environment surrounding the
frequently mutated residue Asp816 in the autoinhibited and
activated c-Kit kinase structures. A, view of the structural
environment surrounding Asp816 in the autoinhibited kinase
structure. Asp816 is situated between the P-loop and a short
region of 3[10] helix where the negatively charged Asp side
chain can stabilize the positively charged helical dipole. B,
view of the structural environment surrounding Asp816 in the
activated kinase structure. Arg815 and Ile^817 form  -sheet
hydrogen bonding interactions with Ile^79 and Asn787 of the
C-lobe to stabilize the activation loop in an extended
conformation.
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