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Figure 10.
Figure 10 The model for binding of MK(62 -104) dimer on the
heparin 20mer units with two conformations. (A) The model for
heparin and MK(62 -104) head-to-head dimer complex (blue, basic
residues; red, acidic residues; green, Gln; and pink, oxygens of
sulfate groups). Positively charged clusters (blue dotted
circles) of MK(62 -104) fit to negatively charged clusters (pink
dotted circles) of heparin. (B) The opposite surface of MK(62
-104) to that shown in (A). The acidic residues of MK(62 -104)
are localized opposite the heparin-binding surface. Gln95 which
is attacked by transglutaminase is exposed opposite to the
heparin-binding surface and is in close proximity to Lys63 on
the counterpart. Lys63 is thought to be an amine donor in the
transglutaminase reaction. (C) Side view of (A). The sulfate
groups are localized on the right and left sides of the heparin
molecule. Basic charged clusters in MK(62 -104) dimer fit the
clusters of sulfate groups.
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