Figure 4.
FIG. 4. Superposition of the native and inhibitor-bound
ACE2 structures. A, the 409 -carbon atoms
corresponding to subdomain II of the native and inhibitor-bound
ACE2 structures were superimposed with an r.m.s. deviation of
1.41 Å. Native ACE2 is colored red, and inhibitor-bound
ACE2 is colored green. The zinc ion is shown as a yellow sphere,
and the inhibitor MLN-4760 is shown in a ball-and-stick
rendering with default atom coloring: gray, carbon; blue,
nitrogen; red, oxygen; green, chlorine. This view is looking
down the length of the active site cleft and is rotated 90°
from that shown in Fig. 3. This perspective illustrates the 16°
hinge-bending movement of subdomain I relative to subdomain II
that occurs upon inhibitor binding to ACE2. B, shown is a
close-up view of the active sites of the superimposed native
(red) and inhibitor-bound (green) ACE2 structures. This is the
same superposition of subdomain II for both structures as
described for A. In this perspective, the residues of subdomain
I within the active site are shown to move upon inhibitor
binding relative to those in subdomain II. The inhibitor
MLN-4760 is shown in stick rendering with the same atom color
code as described for A. The average movement for residues near
the active site is 6-9 Å. The yellow spheres are the two
positions of the zinc atom in the native and inhibitor-bound
structures. This figure was prepared using MOE 2003.02 software
(Chemical Computing Group, Inc.).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
17996-18007)
copyright 2004.
-carbon atoms
corresponding to subdomain II of the native and inhibitor-bound
ACE2 structures were superimposed with an r.m.s. deviation of
1.41 Å. Native ACE2 is colored red, and inhibitor-bound
ACE2 is colored green. The zinc ion is shown as a yellow sphere,
and the inhibitor MLN-4760 is shown in a ball-and-stick
rendering with default atom coloring: gray, carbon; blue,
nitrogen; red, oxygen; green, chlorine. This view is looking
down the length of the active site cleft and is rotated 90°
from that shown in Fig. 3. This perspective illustrates the 
16°
hinge-bending movement of subdomain I relative to subdomain II
that occurs upon inhibitor binding to ACE2. B, shown is a
close-up view of the active sites of the superimposed native
(red) and inhibitor-bound (green) ACE2 structures. This is the
same superposition of subdomain II for both structures as
described for A. In this perspective, the residues of subdomain
I within the active site are shown to move upon inhibitor
binding relative to those in subdomain II. The inhibitor
MLN-4760 is shown in stick rendering with the same atom color
code as described for A. The average movement for residues near
the active site is 6-9 Å. The yellow spheres are the two
positions of the zinc atom in the native and inhibitor-bound
structures. This figure was prepared using MOE 2003.02 software
(Chemical Computing Group, Inc.).