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Figure 4.
Figure 4 Features of papain-like exopeptidases. A view towards
the active site clefts of superimposed papain-like proteases.
The underlying molecular surface of cathepsin L, shown in white,
is used to demonstrate an endopeptidase active site cleft, which
is blocked by features of the exopeptidase structures. The
surface of the catalytic cysteine is colored in yellow. Chain
traces of cathepsins B, X and H are shown in green, cyan and
purple, respectively. Chain traces of papain-like domains of
DPPI are shown in dark blue, whereas for the chain trace of the
exclusion domain the color code is the same as in Figure 1. The
bleomycin hydrolase chain trace is not shown for reasons of
clarity, although its C-terminal residues superimpose almost
perfectly with the C-terminal residues of the cathepsin H
mini-chain (purple).
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