Figure 2.
Figure 2. Comparison of CA^N loop conformations. CA^N
residues 86 -93 are shown as a stick representation with side
chains truncated to the C atom
(except for proline) and carbon atoms colored yellow or orange
(trans) and green (cis). For all figures, the minor (20%
occupied) cis conformations of AMA-A and AMA-A' are not shown
unless explicitly stated. CypA is shown in a ribbon
representation with the Arg55 side chain shown explicitly. (a)
Stereo view showing all eight CA^N structures that adopt the
trans conformation. The four structures that contain Gly89 are
colored yellow; the four Ala89 structures are colored orange.
(b) Same as a but for all eight cis CA^N structures. (c)
Comparison of AAG-A (trans, yellow) and AMG-A (cis, green). (d)
Same as c, but top view. CypA molecular surface colored red. A
model for the transition state is shown with the carbon atoms
colored white. Hydrogen bonds between CypA Arg55 and CA^N Pro90
N and O atoms are shown as dashed lines.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
475-481)
copyright 2003.
atom
(except for proline) and carbon atoms colored yellow or orange
(trans) and green (cis). For all figures, the minor (20%
occupied) cis conformations of AMA-A and AMA-A' are not shown
unless explicitly stated. CypA is shown in a ribbon
representation with the Arg55 side chain shown explicitly. (a)
Stereo view showing all eight CA^N structures that adopt the
trans conformation. The four structures that contain Gly89 are
colored yellow; the four Ala89 structures are colored orange.
(b) Same as a but for all eight cis CA^N structures. (c)
Comparison of AAG-A (trans, yellow) and AMG-A (cis, green). (d)
Same as c, but top view. CypA molecular surface colored red. A
model for the transition state is shown with the carbon atoms
colored white. Hydrogen bonds between CypA Arg55 and CA^N Pro90
N and O atoms are shown as dashed lines.