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. Author manuscript; available in PMC: 2013 Jul 11.
Published in final edited form as: Nat Biotechnol. 2012 Jan 15;30(2):159–164. doi: 10.1038/nbt.2106

Figure 2.

Figure 2

Analysis of disease-associated mutations with respect to interaction interfaces. (a) Odds ratios for the distribution of in-frame mutations in different locations on proteins in hSIN. **P < 10−20. P-values calculated using Z-tests for the log odds ratios. Error bars indicate ± SE. (b) Odds ratios for the distribution of truncating mutations in different locations on proteins in hSIN. (c) Odds ratios for the distribution of non-synonymous SNPs in different locations on proteins in hSIN. (d) Comparison of hSIN with mutations known to modify protein-protein interactions. (e) Illustration of MLH1 and PMS2 interaction interfaces. Colored stars indicate locations of experimentally tested in-frame mutations and SNPs. (f) Effects of in-frame mutations and SNPs on the MLH1-PMS2 interaction tested by Y2H. Flag tagged wild-type and mutant MLH1 were expressed in HEK293T cells, western blot analysis showed similar levels of MLH1 proteins. γ -tubulin was used as a loading control.