Figure 3.

Sequence alignment of RACK1A from A. thaliana (GI:30685669) versus RACK1 from Homo sapiens (GI:83641897), Drosophila melanogaster (GI:24582618), and S. cerevisiae (GI:6323763), as well as a structural alignment with respect to the crystal structure of G_β in complex with G_α and G_γ (PDB ID code 1GP2). Secondary structural elements in RACK1A are shown above the alignment and colored according to the ribbon diagram in Figure 1B. Identity between RACK1A from A. thaliana and human RACK1 versus the other proteins is listed at the end of the alignment. Residues conserved in all RACK proteins shown are marked with an asterisk below the residue. Residues in G_β that are structurally similar to residues in RACK1A are capitalized. Residues of G_β that line the interface with G_γ interface are colored red. Residues lining the interface with G_α are colored green. Tyrosine RACK1 residues predicted to be phosphorylated are colored purple and the predicted sumoylation site of human RACK1 is underlined.