Figure 4.

Docking Studies. Upper panel. Sequence alignment, generated with ClustalW2 [36] of Ship2-Sam, EphA2-Sam and Arap3-Sam. Residues in the helices are colored in blue on the primary sequence of Ship2-Sam and red on the primary sequences of EphA2-Sam and Arap3-Sam. The Shiptide region is indicated. Underlined residues on the EphA2-Sam and Arap3-Sam sequences are the amino acids used in mutagenesis studies (See also [10]). Lower panel. Comparison between the best scoring Haddock [18] models of the EphA2-Sam/Ship2-Sam (Haddock score: -81.76) [10] (left) and Arap3-Sam/Ship2-Sam complexes (Haddock score: -150.72) (right). Residues which are most affected by binding in our chemical shifts perturbation studies (Δδ > 0.1 ppm) have been colored in yellow on the ribbon representations of the molecules. The side chains of the residues that may contribute to important interactions at the dimer interface are shown as neon representation.

Leone et al. BMC Structural Biology 2009 9:59   doi:10.1186/1472-6807-9-59
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