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Figure 1.
Figure 1: Lys 17 alters the apo and Ins(1,3,4,5)P[4]-complexed
AKT1 PHD structure. a, In apo wild-type PHD, an ionic
interaction between Glu 17 and Lys 14 (line) fills the binding
pocket. b, E17K PHD apo with Lys 17 turned away from Lys 14. c,
E17K PHD with Lys 17 involved in new hydrogen bonds (dashed
lines) with a water molecule (orange sphere), interposed with
the D6-hydroxyl group, and the D5-phosphate of Ins(1,3,4,5)P[4]
(orange). Lys 17 also forms a new hydrogen bond with the
hydroxyl of Tyr 18. The D1-phosphate forms a hydrogen bond with
the amide of Tyr 18, similar to the wild-type PHD. Distances
shown are in angstroms.
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