Loops Govern SH2 Domain Specificity by Controlling Access to Binding Pockets

Tomonori Kaneko, Haiming Huang, Bing Zhao, Lei Li, Huadong Liu, Courtney K. Voss, Chenggang Wu, Martin R. Schiller, Shawn Shun-Cheng Li*

*To whom correspondence should be addressed. E-mail: sli{at}uwo.ca

This PDF file includes:

• Fig. S1. Representative SH2 domain structures alone or in complex with peptides.
• Fig. S2. Stereo representation of the crystal structure of the BRDG1 SH2 domain–NTAL complex.
• Fig. S3. Contact area per residue of the NTAL pTyr¹³⁶ peptide with the BRDG1 SH2 domain.
• Fig. S4. The conserved hydrogen bonding network at P+1.
• Fig. S5. Structure-based sequence alignment of a nonredundant group of 63 SH2 domains.
• Fig. S6. Specificity switch by loop mutagenesis.
• Fig. S7. Schematic description of the binding pockets in the Fyn SH2 domain and the loop-deletion mutants.
• Table S1. Crystallographic statistics.
• Table S2. Dissociation constants of SH2-peptide interactions measured by fluorescence polarization.
• Table S3. Peptide binding assays using different BRDG1 SH2 domain constructs.
• References

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Other Supplementary Material for this manuscript includes the following:

• Interactive figures. JMOL representations of the structures shown in Fig. 3A.

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© 2010 American Association for the Advancement of Science