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Figure 7.
Figure 7. Steric clash of AA and sF on AB. The AA:AB(ATP)
complex is shown, viewed parallel with the dimer 2-fold axis, as
in Figure 2 (top), along with the corresponding position of sF
from the sF:AB(ADP) complex.11 AA and sF are shown as orange and
red a-carbon backbone worms, respectively. AB is shown as a
molecular surface. AB1 is colored cyan, AB2 is colored green,
except the surface of AB interacting with AA (4 Å cutoff),
is colored orange and the surface interacting with sF is colored
pink. The surface interacting with both binding partners
(overlap) is colored purple. Residues of AB noted as important
for docking and induced release are colored red and labeled, and
the corresponding residues on AA are drawn as stick. These pairs
include AB-Arg20:AA-Glu21, AB-Ile112:AA-Leu90, AB-ATP:AA-Ser58,
AB-Glu104:AA-Arg67. Note that the clash occurs in the area of
AB-Arg20 between AA and sF as previously predicted.[11.]
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