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Figure 5.
Figure 5. Stereo View of Interaction of VCP with HeparinA
Cα trace of residues 213–242 of VCP is shown in orange.
Carbohydrate is shown with carbons colored gray; oxygen, red;
nitrogen, blue; and sulfur, yellow. Side chains of the four
basic residues of acidic and basic FGF and VCP that were
superimposed are shown in red, magenta, and cyan, respectively.
VCP side chains are labeled. The figure was composed using a
rigid body transformation of VCP main chain on to the basic FGF
heparin binding segment. The side chains of the Lys residues in
VCP have been rotated to point toward the heparin fragment. The
side chain of Lys 214 is beyond hydrogen bonding distance from
heparin as currently modeled. Main chain movements of 1–2
Å will be required to bring its side chain within
interacting distance.
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