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. 2003 Jun;14(6):2385–2398. doi: 10.1091/mbc.E02-11-0735

Figure 6.

Figure 6.

Structure of the GGA1 appendage domain and comparison with the γ and α appendages. (a) Structure of the GGA1 appendage shown as a ribbon diagram. The residues that have been mutated in GGA1 for protein–protein interaction studies are indicated as ball and stick representations. (b) Cα overlay of the GGA1 appendage (green) with the γ appendage (orange) (Kent et al., 2002) and the α appendage (magenta) (Owen et al., 1999). The γ appendage overlays the GGA1 appendage with an rmsd of 1.2 Å > 113 Cα atoms. Figures were made with AESOP (Collins et al., 2002). (c) Structure-based sequence alignment of GGA1 and γ appendage domains. The secondary structure of the GGA1 appendage is shown as green arrows, and conserved residues are highlighted in gray. The region shown to bind p56 by mutagenesis is boxed in red.