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. Author manuscript; available in PMC: 2016 Oct 1.
Published in final edited form as: Biochim Biophys Acta. 2015 Jun 12;1853(10 0 0):2560–2569. doi: 10.1016/j.bbamcr.2015.06.002

Figure 7. Comparison of the current and revised model for the interaction of GRB2 with SH3 domain ligands.

Figure 7

The current model suggests that PxxPxR motifs are critical for the interaction of GRB2 with SH3 domain ligands. These interactions are low affinity and have variable ligand specificity driven by an unknown mechanism, making the poor clinical targets. Our revised model indicates that the interaction of GRB2 with SH3 domain ligands is driven by multiple contacts outside of the PxxPxR motifs. These interactions are high affinity and have ligand specificity based on sequence differences; thus, these interactions could potentially be targeted for clinical intervention.