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Figure 2.
Figure 2 Comparison of Ins(1,3,4,5)P[4] binding to the PH
domains of PDK1, DAPP1 and PKB  .
Interactions of Ins(1,3,4,5)P[4] (marine) with protein residues
(green in PDK1, orange in DAPP1/PKB )
in the phosphoinositide-binding site are shown in a stereo
representation. Hydrogen bonds are indicated as black dotted
lines, and conserved water molecules are shown as yellow
spheres. (A) Protein -ligand interactions of PDK1 PH domain with
Ins(1,3,4,5)P[4]. A layer of ordered water molecules (coloured
in magenta) separates the ligand from VL1, only one of which is
conserved in other PH domain structures (coloured in gold). (B)
Ins(1,3,4,5)P[4] binding to DAPP1 (pdb-id 1fao; Ferguson et al,
2000). The D5-phosphate is closely enveloped by VL1. (C)
Ins(1,3,4,5)P[4] binding to PKB (pdb-id
1h10; Thomas et al, 2001). The ligand is rotated and VL1
contacts the D1-phosphate, while the D5-phosphate is solvent
exposed. (D) Overlay of the structures of the PDK1 (green),
DAPP1 (orange) and PKB (blue)
PH domains. The Ins(1,3,4,5)P[4] ligand and the layer of ordered
water molecules of PDK1 are shown, and coloured according to (A).
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