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Figure 1.
Figure 1. Crystal Structure of the
Rac2^G12V(GTPγS)/PLCγ[2]spPH Complex
Domain organization
of PLCγ[2] (A) shows domains common to all families (nPH,
EF-hands, catalytic, and C2) and domains specific to PLCγ
family (nSH2, cSH2, SH3, and spPH); spPH is shown in orange.
Overview of the Rac2^G12V(2-177) GTPγS/PLCγ[2]spPH complex
structure (B). Surface topology (shown as translucent surfaces)
and ribbon representation of the complex show the spPH domain in
orange and the Rac2 molecule in blue. The Rac2 switch I region
is shown in green, and the switch II region is shown in magenta.
The GTPγS molecule bound to Rac2 is in ball-and-stick
representation. Close-up of the interaction interface is viewed
from the side with important amino acid residues of both Rac2
and spPH represented as ball and sticks (C). Also shown is a
close-up from above with important Rac2 amino acid residues
(ball-and-stick representation) and the spPH surface (D). The
hydrophobic cleft into which Rac2 residues Val36 and Phe37
protrude can be clearly seen. The summary of interactions at the
interface is illustrated schematically highlighting the
predominant types of bonding between the two species in the
complex (E).
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