Skip to main content
. 2021 Dec 2;12:7047. doi: 10.1038/s41467-021-27343-z

Fig. 2. Crystal structure of the intracellular region of the EphA2 S897E/S901E phosphomimetic mutant.

Fig. 2

a Overview of the asymmetric unit containing a single EphA2 molecule in an elongated conformation; resolution 2.8 Å. The kinase domain is shown in blue and the SAM domain in cyan. The structure includes most of the juxtamembrane segment (JM) and the kinase domain, the full activation loop (including residues L760-I779, which are not defined in the WT structure), and the SAM domain (residues V909-L965). Parts of the linker region and N-terminus of the SAM domain (residues 900–908, dashed line) and the C-terminal tail (K966-I976) are not visible in the structure due to missing electron density. b Comparison of the resolved linker regions in the structures of EphA2 WT molecule B (colored as in Fig. 1d) and the S897E/S901E mutant (blue), highlighting key differences in the linker structures. Key residues are shown as sticks and labeled. R890 and the phosphomimetic E897 in the S897E/S901E structure form a salt bridge (green dashes). The SAM domains are omitted for clarity.