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Figure 4.
Figure 4. Structural changes of the PH domain. (a)
Structural comparison of the tandem DH/PH domains. Collybistin
II, Tiam 1, Dbs, intersectin and Sos1 were aligned according to
the conserved regions of their DH domains. In collybistin II,
the PH domains are colored green in the open conformation and
gray in the closed conformation. (b) Collybistin II in the open
conformation. Residues that lose solvent-accessible surface area
upon transition to the closed conformation are highlighted with
positively charged residues in blue, negatively charged residues
in red, polar residues in cyan and non-polar residues in gray.
(c) Collybistin II in the closed conformation (same color code).
An additional salt-bridge between Asp136 (red) and Lys379 (blue)
in the closed conformation is visible on the bottom of the DH/PH
domain interface. (b) and (c) are aligned according to their PH
domains. Residues highlighted in (b) with an arrow are
disordered in the open conformation.
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