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Figure 2.
Figure 2 Stereo plot of the activation domain environment of
sc-tPA involving residues of the activation pocket, the
activation loop and Lys156. Lys156 (blue) stabilizes the active
conformation of sc-tPA via formation of a salt bridge with
Asp194 (red). The strength of this interaction is presumably
increased by the concerted solvent shielding effect of the (red)
activation loop and of the hydrophobic residues Ile16, Phe21 and
His144 (yellow). Lysines 17 and 143, which were considered
potential activators of sc-tPA (Wallén et al., 1983; Petersen et
al., 1990) are also shown (blue). Residues His188, Arg186A and
Asn186F of the 186 loop (yellow) are presumed to be responsible
for the conformational stabilization of this loop.
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