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Figure 4.
Figure 4 (a) Interactions between DPLA[2] and the designed
peptide LAIYS. The peptide residues are indicated with a `P' in
parentheses. The critical interactions between Tyr(P) OH and
His N  1
and Asp O 1,
including other hydrogen bonds between peptide and protein, are
indicated by dotted lines. The figure was drawn with MOLSCRIPT
(Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24,
946-950.]) and Raster3D (Merritt & Murphy, 1994[Merritt, E. A. &
Murphy, M. E. P. (1994). Acta Cryst. D50, 869-873.]). (b)
LIGPLOT (Wallace et al., 1995[Wallace, A. C., Laskowski, R. A. &
Thornton, J. M. (1995). Protein Eng. 8, 127-134.]) showing the
schematic representation of the interactions between the peptide
LAIYS and protein molecule. (c) GRASP (Nicholls et al.,
1991[Nicholls, A., Sharp, K. & Honig, B. (1991). Proteins, 11,
281-296.]) representation of the binding cavity and the
hydrophobic channel. The peptide LAIYS is almost completely
buried in the pocket. Two key hydrogen bonds involving His48 and
Asp49 of the protein with peptide Tyr OH are also indicated by
dotted lines.
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