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Figure 3.
Figure 3. Conformational Changes Induced within the DH/PH
Domains of Dbs upon Binding a GTPaseThe structure of Dbs·RhoA
(transparent) was superimposed on the GTPase-free form of Dbs
(molecule B) using DH domain residues. Significant interactions
between RhoA and the b3/b4 loop as well as a6 serve to reduce
the conformational heterogeneity between DH and PH domains and
result in the ordering of the b3/b4 loop and the tilting of the
PH domain toward the GTPase.
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