Optimization of specificity in a cellular protein interaction network by negative selection
Supplementary Figure 1
Figure S1. Binding profiles of all yeast SH3 domains from phage display experiments
Supplementary
Figure 2
Figure S2. Construction and alignment of the Sho1 SH3 domain replacements
Supplementary
Figures 3-5
Figure S3. Sequence dendrogram of all the SH3 domains used in this study
Figure S4. Osmoresistance correlates with SH3-peptide affinity
Figure S5. Chimeric (swapped SH3) Sho1 constructs do not change in expression
levels or subcellular localization
Supplementary Figures 6-8
Figure S6. Construction of Pbs2 polyproline motif mutations
Figure S7. Sampling single base pair missense mutations in the Pbs2 proline-rich
peptide
Figure S8. Analysis of peptide binding to SH3 domain arrays
Supplementary
Figures 9-10
Figure S9. Location of mutated Pbs2 peptide residues in an SH3-peptide
complex
Figure S10. Analysis of cross-reaction for other putative physiologically
relevant yeast SH3 domain/ligand pairs
Supplementary
Figure 11
Figure S11. Controlling for growth and expression
Abstract
PDF
Commentary
in Nature by Drew Endy and Michael B. Yaffe