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Figure 2.
Figure 2. Interactions between ARL2-GTP and BART
(A) A
stereo view showing the interactions between ARL2 and BART at
interface I. Helix α1 of ARL2 (cyan) is embedded in a
hydrophobic cleft formed by helices α3, α4, and α5 of BART
(green).
(B) A stereo view showing the interactions between
ARL2 and BART at interface II. The switch regions of ARL2
(switches I and II and the inter-switch region in magenta,
orange, and blue, respectively) have both hydrophobic and
hydrophilic interactions with the N terminus of helix α3 and
the following loop of BART (green). The hydrogen-bonding
interactions are indicated by dashed lines.
(C) A schematic
diagram showing the hydrophobic contacts between ARL2 and BART.
(D) A schematic diagram showing the hydrogen-bonding
interactions between ARL2 and BART.
(E) In vitro binding
assay of the wild-type and mutant ARL2 with the GST-fused
wild-type BART. GST cannot bind to ARL2 and thus was used as the
negative control.
(F) In vitro binding assay of the
wild-type ARL2 with the GST-fused wild-type and mutant BART.
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