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Figure 9.
Figure 9. Topography of the docking sites on calcineurin and
PP1. a, Views from the end of each site that would be occupied
by the N-terminal residues of the corresponding peptide,
illustrating the rather different surface topographies. F299 and
other labelled residues in the foreground surround the proline
pocket. b, Views from the end of each site that would be
occupied by the C-terminal residues of the corresponding
peptide, illustrating the similar topographies of the
hydrophobic troughs in the two proteins. The trough in
calcineurin, however, is closed off by the side-chains of F299
and P300, thereby forming the Ile8 recess.
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