|
Figure 1.
Figure 1. Structure of PKB[α]PH Complexed to
Ins(1,3,4,5)P[4](A) A ribbon drawing of the
PKB[α]PH-Ins(1,3,4,5)P[4] complex, with the seven β strands
(labeled β1–7) shown in blue and the α helices (labeled
α1–2) shown in red. Ins(1,3,4,5)P[4] is shown as purple
carbons. The side chains of residues interacting with this
molecule are shown as gray carbons. The basic residues thought
to interact with the membrane have their side chains shown as
sticks with green carbons. The negatively charged residues on
VL2 that are hypothesized to interact with the kinase domain are
shown as gray-blue carbons.(B) Ribbon diagrams of the
Ins(1,3,4,5)P[4] binding sites of PKB, GRP1, DAPP1, and BTK. The
Ins(1,3,4,5)P[4] is shown as purple carbons. For the
PKB-Ins(1,3,4,5)P[4] structure, the experimental electron
density map from SOLVE after density modification is shown in
orange (contoured at 2.25σ). Residues that are hydrogen bonding
the ligand are shown as sticks with gray carbons. Hydrogen bonds
are shown as black dotted lines.
|
