|
Figure 6.
FIG. 6. The hydrophobic knuckle. a, presence of a large
non-polar surface exposed to the solvent (potential surface map,
calculated by GRASP (89)), formed by hydrophobic residues
surrounding Lys122, and constituting the hydrophobic knuckle. In
all cases, Lys122 interacts with the Cys29-Gly30 peptide bond,
and a ligand is bound to the hydrophobic channel. Positive
charges surround the base of the knuckle. b, the knuckle can
also be observed in ligand-free structures that present the
canonical conformation for the C-terminal region, where Lys122
interacts with Cys29-Gly30 peptide bond. c, structures where
Lys122 is exposed to the solvent, the hydrophobic knuckle is not
observed.
|
