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. 2003 May 5;100(10):5688–5693. doi: 10.1073/pnas.1031524100

Figure 4.

Figure 4

The acidic hydrophobic motif in cterFCP. (A) Alignment of the amino acids in the H1′ α-helix of human FCP1-(E945–M961) with corresponding sequence in mouse FCP1, Xenopus laevis FCP1, and yeast FCP1. Residues that are important for interactions with RAP74 are boxed in gray. A consensus sequence is shown below. The mouse and Xenopus sequence are from databases and the mouse sequence is partial. (B) Varying concentrations (0.1–15 μM) of cterRAP74-(436–517) was incubated either with 1 μM GST-cterFCP (ELNDLM) or 1 μM GST-cterFCPmut (AANDLM) immobilized on GSH resin as described in Methods. In the GST lane, 15 μM of purified cterRAP74 was incubated with 1 μM of immobilized GST as a control for nonspecific binding. The input lane is 10% input of purified cterRAP74.