Figure 3.
FIGURE 3. Stereo views of the structure of monomeric AT
reveals a novel RCL conformation and contacts. A, superimposed C
traces of native AT
from crystals of the heterodimer (gray) and of monomeric AT
(oriented as in Fig. 1A) reveal regions of conformational
difference. Monomeric AT is colored according to C root
mean squared deviation (yellow to red, from 1 to 6 Å) with
the active component of 1E04 ( -glycoform). Disulfide
bonds are shown as green rods, and the P1 residue is indicated
by a blue ball. Regions that differ most significantly are the
RCL (top) and the heparin binding site (lower right). B, the RCL
of monomeric AT (from P5 to P3') is shown with corresponding
electron density (contoured at 1 ). C, extensive
intramolecular contacts are observed between the RCL and the
body of AT; those involving the P1 Arg-393 are indicated by
dashed lines.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
35478-35486)
copyright 2006.
traces of native AT
from crystals of the heterodimer (gray) and of monomeric AT
(oriented as in Fig. 1A) reveal regions of conformational
difference. Monomeric AT is colored according to C 
-glycoform). Disulfide
bonds are shown as green rods, and the P1 residue is indicated
by a blue ball. Regions that differ most significantly are the
RCL (top) and the heparin binding site (lower right). B, the RCL
of monomeric AT (from P5 to P3') is shown with corresponding
electron density (contoured at 1 
). C, extensive
intramolecular contacts are observed between the RCL and the
body of AT; those involving the P1 Arg-393 are indicated by
dashed lines.