The active EGFR kinase domain dimerizes through an asymmetrical interface, and it is even more active when an asymmetric dimer is formed. Negative-stain EM analysis of EGFR now shows that the kinase domains of a dimer can exist in three different states depending on the presence of ligand, mutations and inhibitors, whereas the receptor ectodomain remains in just one conformation.
- Li-Zhi Mi
- Chafen Lu
- Timothy A Springer
