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Figure 1.
Figure 1. Overall structure of dimeric human granzyme A. (a)
Ribbon diagram of dimeric human GzmA. The secondary structural
elements are colored in a gradient from N to C terminus. The
Ser195-His57-Asp102 catalytic triad and P1 coordinating Asp189
are shown in ball and stick (carbons, light green) as is the
D-Phe-Pro-Arg-chloromethylketone (carbons, cyan). The disulfide
linkage is depicted as space-filling model for residue 93 and
its symmetry mate. A sulfate ion contributed from the
crystallization solution is bound at the base of loop 184-B -197
by Arg186 and Arg188. (b) Surface representation mapped with
potentials shows the overall positive charge of the molecule
reflected by its pI > 9 and the distinct negative charge of
Asp189 emanating from the S1 pocket.
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