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Figure 7.
Figure 7. PP1 Leaves Unfilled a Cavity in Inactive Hck(A)
Structure of the PP1-binding region in inactive Hck. PP1 binding
creates a cavity (yellow surface) in the back of the ATP-binding
site, where two well-ordered water molecules (W1 and W2) are
found.(B) The same cavity (yellow) viewed from the top of the
N-terminal lobe of the catalytic domain. The collapse of this
cavity in active Lck is indicated by showing helix αC as found
in the structure of Lck (PDB code 3lck; [45]), drawn in orange.
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