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Figure 1.
Figure 1 Stereo ribbon plot of the catalytic domain of sc-tPA in
'standard' orientation. The inhibitor
(dansyl-Glu-Gly-Arg-chloromethylketone) shown by green sticks is
covalently bonded to Ser195 and His57 of the catalytic triad.
Key sc-tPA residues are shown as yellow sticks: Asp102, His57
and Ser195 of the catalytic triad; Asp189 at the base of the S1
specificity pocket; and Asp194 and Lys156 which form a salt
bridge in the activation pocket. The red ribbon shows the
conformation of the N-terminal activation loop which includes
the plasmin cleavage site. Some loops arranged around the active
site are labelled: the mainly disordered 37 loop and the 110
loop to the east; the partially disordered 186 loop to the
south-west is in proximity to the activation loop. The figure
was made with SETOR (Evans, 1993).
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