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. Author manuscript; available in PMC: 2018 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Oct 21;1864(1):31–38. doi: 10.1016/j.bbamcr.2016.10.011

Figure 1.

Figure 1

The four EphA2 constructs investigated in this work to elucidate the role of the EphA2 SAM domain in receptor dimerization. For these measurements we used both the wild-type and the EphA2 L223R/L254R/V255R mutant, which has lower dimerization ability due to extracellular mutations in a receptor-receptor interface. Both EphA2 wild-type and mutant were analyzed in their full-length version and in a version lacking the SAM domain.