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Figure 3.
Figure 3. Structure of the A1-Botrocetin Complex(A) Stereo
view (Ca tracing) of the complex. The current model includes 199
residues from 502 to 700 of the mutant A1 domain, 133 (119)
residues of the a (b) subunits of botrocetin, and 94 water
molecules. There is no electron density for the loop (residues
55-60 in the b subunit). The A1 domain is in blue; the a and b
subunits of botrocetin are in pink and green, respectively.
Gain-of-function mutations are shown as blue balls;
loss-of-function mutations are shown in red; loss of botrocetin
binding mutations are shown in yellow. The I546V mutation site
is shown as a green ball.(B) Space-filling model of the complex
with mutation sites indicated; same view as in (A). The NMC-4
antibody (V[H]-V[L] dimer) is shown as a semitransparent
molecular surface.(C) Electrostatic surface potential contoured
from -15 (red) to +15 (blue) kT e^ -1. The figure was made using
RASTER3D [30] and GRASP [32].
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