TABLE 1.
Residues on EphA4 that were found to interact with compound 1 in solution by Qin et al
| EphA4 residuea | Corresponding EphA2 residueb | Interaction data for EphA4c |
|---|---|---|
| I31 | I58 | NMR + HADDOCK |
| M32 | M59 | NMR + HADDOCK |
| I39 | I64 | NMR |
| Q43 | S68 | NMR + HADDOCK |
| D123 | D148 | NMR |
| I131 | F156 | NMR + HADDOCK |
| G132 | E157 | NMR + HADDOCK |
a
As numbered in reference 35, starting at position 28 as the first amino acid.
b
Corresponding residues on EphA2 were determined by us using the BLAST algorithm and were confirmed visually in the structure to match the positions on EphA4.
c
From reference 35. Only residues that were identified by NMR and could be fitted into a computational docking model (nuclear magnetic resonance [NMR] plus HADDOCK) were considered real interactions by Qin et al.