Skip to main content
Figure 2 | BMC Structural Biology

Figure 2

From: Quantifying information transfer by protein domains: Analysis of the Fyn SH2 domain structure

Figure 2

Change in mutual information per residue and most significant cluster. Binding the peptide with phosphorylated tyrosine to the SH2 domain results in a change in mutual information residue-residue interactions. (A) This panel shows the change in mutual information for each pairwise interaction. Clearly most residues remain unaffected. A number of residues at particular positions experience the strongest effect. (B) Most residues experience almost no change in mutual information. The inset shows the distribution in the tail starting with a change in mutual information bigger than 0.5 (noise level) (C) Clustering the residues using the change in mutual information as similarity measure (see Methods), results in a cluster of highly coupled residues, located in the binding pockets and near the kinase-linker region of the SH2 domain. All molecular graphics created with YASARA http://www.yasara.org and PovRay http://www.povray.org.

Back to article page