Figure 5.
FIG. 5. A comparison of the low resolution
three-dimensional reconstruction of EV12-DAF[34] (A) and a
space-filling representation of the EV12-DAF[34] complex (B),
generated using the crystallographic co-ordinates for EV11 and
DAF[34]. Radial depth-cueing emphasizes the distance between
atoms or regions of density and the center of the virion such
that dark colors are close to the center and light colors are
farther away. EV12 (and EV11) is colored in shades of blue,
whereas DAF[34] is colored in green. A space-filling
representation of the EV7-DAF[1234] complex (30) (C) highlights
the different orientation of DAF bound to these two viruses. The
model deposited under PDB code 1M11 [PDB]
contains -carbon atoms only;
this view is therefore rendered with the atomic radii for each
atom set to 3.5Å. EV7 is colored in shades of purple, and
the receptor is in red. A close-up view of DAF[34] shown as in
panel B but rotated 180^o about a vertical axis exposes the
residues buried in the virus-receptor complex (D). Residues are
colored according to their contribution to the total contact
area ( 840 Å2); yellow (1
< 5%), orange (5 < 9%), and red (9%+). A close-up view of EV11
without the receptor in place exposes buried residues on the
surface of the capsid that are colored according to the same
scheme (E); the biological protomer is indicated.
-carbon atoms only;
this view is therefore rendered with the atomic radii for each
atom set to 3.5Å. EV7 is colored in shades of purple, and
the receptor is in red. A close-up view of DAF[34] shown as in
panel B but rotated 180^o about a vertical axis exposes the
residues buried in the virus-receptor complex (D). Residues are
colored according to their contribution to the total contact
area ( 
840 Å2); yellow (1
< 5%), orange (5 < 9%), and red (9%+). A close-up view of EV11
without the receptor in place exposes buried residues on the
surface of the capsid that are colored according to the same
scheme (E); the biological protomer is indicated.