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. 2017 May 24;292(27):11361–11373. doi: 10.1074/jbc.M117.789883

Figure 7.

Figure 7.

A, schematic representation of the Cdc42–ACK structure (PDB entry 1CF4). Cdc42 is shown in gray, with hydrophobic residues (Ala, Gly, Val, Ile, Leu, Phe, and Met) colored orange. ACK is shown in blue, and its N terminus is labeled. B, van der Waals surface of Cdc42–ACK structure shown in the same orientation as in A. The van der Waals surface of Cdc42 is solid, whereas ACK residues 448–489 are shown as a blue mesh. C, as in B, but with the Cdc42–ACK structure rotated 90° around the vertical, anti-clockwise. D, as in B, but with the Cdc42–ACK structure rotated 180° around the vertical, anti-clockwise. E, as in B, but with the Cdc42–ACK structure rotated 270° around the vertical, anti-clockwise. F, van der Waals surface of Cdc42·GMPPCP shown in gray, with hydrophobic residues (Ala, Gly, Val, Ile, Leu, Phe, and Met) colored orange. Leu-174, Leu-177, Ile-46, Gly-47, and Gly-48 are shown in red (PDB entry 2QRZ). Switch I residues are colored blue. G, van der Waals surface of Rac1 Q61L·GMPPNP shown in gray, with hydrophobic residues (Ala, Gly, Val, Ile, Leu, Phe, and Met) colored orange. Arg-174 is shown in green (PDB entry 2GZL). Switch I residues are colored blue.