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Figure 1.
Fig. 1. Overall structure of neuropsin. a, ribbon
representation of neuropsin. Seven-stranded  -sheets (the
top and bottom halves) are sandwiched with the catalytic triad
at the cleft of the -sandwich.
The surface loops (A-H) forming the substrate-binding site are
colored with labels. Six disulfide bonds are shown by bridges in
white, and the disulfide bond (SS3), which is conserved in
trypsin but not in kallikrein, was labeled. Loop D is the
kallikrein loop that has an N-glycosylated Asn95 with one
visible GlcNAc residue. The side chains of the catalytic triad,
Asp189 at the S1-specific pocket, Lys175 at the S3/4 site,
Glu149 and Asp218 at the rim of the S1 pocket, and Leu40 and
Ile^41 at the S1' site, are also shown with stick
representations with one-letter amino acid labels. b, molecular
surfaces of neuropsin viewed from nearly the same direction of
panel a. Surface electrostatic potentials calculated and
rendered using GRASP (negative potentials are in red and
positive in blue). The S1-S4 and S1' sites and characteristic
surface residues are labeled.
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