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. Author manuscript; available in PMC: 2011 Jun 1.
Published in final edited form as: Traffic. 2010 Feb 27;11(6):732–742. doi: 10.1111/j.1600-0854.2010.01054.x

Figure 1.

Figure 1

A. Schematic of recombinant human Arf proteins used in this paper. B. Modeled structures of recombinant proteins. 1) Ribbon diagram of Arf1 with bound GDP (orange). The N-terminal 17 residues are blue and the C-terminal residues 165–170 are yellow, 171–175 orange, 176–179 red, and 180–181 pink corresponding to the yeast Arf1-CΔ17, CΔ11, CΔ6 and CΔ2 constructs. The Switch 1 region (S1) is shown in dark gray, and the Switch 2 (S2) region in purple. 2) Arf1•GDP with C-terminal HA epitope tag. The backbone ribbon for the HA tag (YPYDVPDYA) is shown in magenta and its two aspartate residues shown in red. The HA tag is positioned near the five lysine and arginine residues, shown in blue, of the Arf1 N- and Cterminal regions. 3) Model of the Arf1-GFP construct with Arf1 shown in green with bound GDP (orange), GFP shown in magenta, and engineered linker shown in light gray. 4) Model of the GST-Arf1 construct with GST shown in magenta, Arf1 shown in green with bound GDP (orange), and engineered linker shown in light gray. C. SDS-PAGE analysis of purified recombinant Arf1 preparations. Arf1, Arf1-HA, Arf1-GFP and GST-Arf1 (3.2 μg protein) were loaded onto lane 1, 2, 3, and 4, respectively, of a 15% polyacrylamide gel. Their molecular weights are 20.7, 21.6, 47.8, and 48.9 kDa.