Figure 1.
Figure 1. (a) Ribbon representation of the hRI-EDN complex,
drawn with the program MOLSCRIPT.58 The hRI molecule has been
coloured purple and the EDN molecule is shown in olive green.
(b) Stereo view of the superposed C^a traces of the hRI-EDN
complex (purple), the pRI-RNase A complex18 (olive green) and
the hRI-Ang complex12 (cyan). Superpositioning was performed by
aligning the RI components of the respective complexes. (c)
Stereo view of the superposition of C^a traces of the two hRI
molecules in the asymmetric unit. hRI from Complex 1 is coloured
purple and the hRI from Complex 2 is shown in blue. (d)
Molecular surfaces of the inhibitor (left panel) and the enzymes
(right panel) from the different RI complexes. The horseshoe was
rotated by vert,
similar 20° from the standard orientation (b) in order to
better show the interface. The enzymes were rotated by about
180°, along the x-axis, from the standard orientation (b) to
show their binding interface. The surfaces have been colour
coded according to the type of contact atoms at the interface.
Non-polar atoms are coloured green, uncharged polar atoms are
shown in blue and charged atoms in red. The program GRASP was
used to draw the molecular surfaces.59
The above figure is reprinted
by permission from Elsevier:
J Mol Biol
(2005,
347,
637-655)
copyright 2005.
vert,
similar 20° from the standard orientation (b) in order to
better show the interface. The enzymes were rotated by about
180°, along the x-axis, from the standard orientation (b) to
show their binding interface. The surfaces have been colour
coded according to the type of contact atoms at the interface.
Non-polar atoms are coloured green, uncharged polar atoms are
shown in blue and charged atoms in red. The program GRASP was
used to draw the molecular surfaces.59