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Updated: May 3, 2026

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
Published on: May 20, 2020
Structure-function relationships and supramolecular organization of the EGFR (epidermal growth factor receptor) on
Sarah R Needham1, Laura C Zanetti-Domingues1, Michael Hirsch1
1*Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxfordshire OX11 0FA, U.K.
Abstract:
Dimerization and higher-order oligomerization are believed to play an important role in the activation of the EGFR (epidermal growth factor receptor). Understanding of the process has been limited by the lack of availability of suitable methods for the measurement in cells of distances in the range 10-100 nm, too short for imaging methods and too long for spectroscopic methods such as FRET. In the present article, we review the current state of our knowledge of EGFR oligomerization, and describe results from a new single-molecule localization method that has allowed the quantitative characterization of the distribution of EGFR-EGFR distances in cells. Recent data suggest the involvement of cortical actin in regulating the formation of EGFR complexes.
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