Superbinder SH2 Domains Act as Antagonists of Cell Signaling

Tomonori Kaneko, Haiming Huang, Xuan Cao, Xing Li, Chengjun Li, Courtney Voss, Sachdev S. Sidhu,* Shawn S. C. Li*

*To whom correspondence should be addressed. E-mail: sachdev.sidhu{at}utoronto.ca (S.S.S.); sli{at}uwo.ca (S.S.C.L.)

This PDF file includes:

• Fig. S1. SH2 domain variants obtained by screening a phage-displayed library.
• Fig. S2. An alignment of the human SH2 domains showing the region for pTyr binding.
• Fig. S3. The specificity and affinity of the Fyn SH2 triple mutant in comparison to those of the wild-type domain.
• Fig. S4. Amino acid combinations of the pTyr-binding pocket in natural SH2 domains.
• Fig. S5. The dynamics of the BC loop and its stabilization in the Src SH2 triple-mutant domain.
• Fig. S6. The structure of the pTyr-binding pocket of the Src SH2 domain triple mutant.
• Table S1. Minimal distances between pocket-forming residues in an SH2 domain and the pTyr residue of the ligand.
• Table S2. A list of biotinylated peptides used for screening the phage-displayed Fyn SH2 domain library.
• Table S3. A list of fluorescein-labeled peptides used for the in-solution binding assay.
• Table S4. Fitting error statistics for the K_d values reported in Table 1.
• Table S5. Fitting error statistics for the K_d values reported in Table 2.
• Table S6. Data collection and refinement statistics for x-ray crystallography.

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© 2012 American Association for the Advancement of Science