Lim Lab | Papers

Optimization of specificity in a cellular protein interaction network by negative selection

Ali Zarrinpar, Sang-Hyun Park, and Wendell A. Lim
Nature 426, 676-680 (2003)

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

Commentary in Nature by Drew Endy and Michael B. Yaffe