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. Author manuscript; available in PMC: 2011 Aug 10.
Published in final edited form as: Biochemistry. 2010 Aug 10;49(31):6687–6695. doi: 10.1021/bi1006223

Figure 2.

Figure 2

Alanine scan for the YSA peptide. (A) IC50 values for the indicated modified forms of the YSA peptide were calculated from curves of inhibition of ephrin-A5 AP binding to immobilized EphA2 Fc. The table shows average IC50 values, calculated from the indicated number of experiments (n). Ala-1 through Ala-12 are the peptides, where alanine replaces the indicated residue. Ala-3 is the original YSA peptide. For peptides Ala-1 and Ala-5 the IC50 values were too high to measure accurately (>100 μM); for the Ala-4 peptide no inhibition was detectable at 100 μM, which is the highest peptide concentration tested (≫100 μM). (B) The histogram shows the IC50 values ± SE. The sequence of the YSA peptide is shown, with the residues identified as critical for binding to EphA2 in bold.