Biomedical Engineering Reference
In-Depth Information
acidity contributed by Ala657 probably lowers the anity for N-terminal
amines and enables FAP to act as both a dipeptidyl peptidase and endo-
peptidase.
122,148
The structural features of FAP are shown in Figure 5.4.
A
B
C
Figure 5.4
Crystal structure of the FAP monomer (PDB code 1Z68). (A) Ribbon
representation of the b-propeller and a/b-hydrolase domains which form
the catalytic pocket and a side opening at their interface, on the right. The
locations of active-site residues Ser624 (dark blue), Ala657 (pink), and
Asn704 (green) of the a/b hydrolase domain, and Arg123 (purple),
Glu203, and Glu204 (cyan) of the b-propeller domain are indicated by
spheres. The N-terminal transmembrane and cytoplasmic portions of FAP
are not depicted; they would be above the molecule. Propeller blades 1 to 8
are coloured yellow, cyan, dark blue, orange, green, purple, blue, and red
respectively, and the hydrolase domain is grey. The molecule is turned
1801 around the vertical axis in image (B). In image (C) the molecule is
rotated 901 around the horizontal axis to show the propeller architecture
viewed from the bottom of the molecule depicted in (A). Image generated
using PYMOL (DeLano WL: http://www.pymol.org).
