Structural Mechanisms of Inactivation in Proteolytically Inactive Serine Proteases from Sarcoptes scabiei - Proteinases as Drug Targets - page 239

D

SMIPP-S-D1

Y200

T145
Q192*

N143*

N

V197

A

180˚

A142
V191

L107

P13

Q

I105

K103

I228
L31

SS1

D98

L97

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Average Variable Conserved

Insufficient data

E

SS2

SS3

Y200

A

180˚

N/D

SS1

Q/H

Figure 10.4 Continued.

SMIPPs (Figure 10.4E); regions of lower sequence conservation show the lar-
gest structural shifts. Interestingly, there are small patches of conserved regions
on the opposite face of the molecule to the active site (Figure 10.4C-E). These
are in regions of good agreement between the SMIPP structures, suggesting
that they may represent potential binding sites or exosites. All but one of the
predicted N-glycosylation sites for both SMIPPs lie within conserved regions
on this face, and this may provide a plausible explanation for the conservation
at these sites (Figure 10.4C and D).