Figure 7 - full size

 

Figure 7.
Fig. 7. Solvent-accessible surface representation of the FKBP12-FK506 complex structure. The surface is color coded with respect to its curvature, from concave (in red) to convex (in blue), as calculated by the program GRASP (Nicholls & Honig, 1992). Side chains for those residues known to be involved in calcineurin inhibition by site-directed mutagenesis studies (Aldape et al., 1992; Yang, Rosen & Schreiber, 1993) are also displayed. A number of suggestive depressions are found n the functionally important region of the complex surrounding the bound ligand, including the 'catcher's mitt' (see text) formed by FK506 and protein residues Asp37, His87 and Ile90. A second depression ivolves residues Arg2 nd Phe46. Ligand-induced conformational changes, or mutations (Aldape et al., 1992; Itoh et al., 1995) in this mobile egion of the protein ould alter the conformation of these surface depressions (or could eliminate them altogether), thereby preventing the binding and inhibition of calcineurin.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1995, 51, 511-521) copyright 1995.