EGFR 3D Molecular Visualization

EGFR, Biologic Animation

aEGFR Receptor Dimer

Protein Description

The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is a transmembrane protein that is a receptor for members of the epidermal growth factor family (EGF family) of extracellular protein ligands. The epidermal growth factor receptor is a member of the ErbB family of receptors, a subfamily of four closely related receptor tyrosine kinases: EGFR (ErbB-1), HER2/neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4). Mutations affecting EGFR expression or activity could result in cancer. Epidermal growth factor and its receptor was discovered by Stanley Cohen of Vanderbilt University. Cohen shared the 1986 Nobel Prize in Medicine with Rita Levi-Montalcini for their discovery of growth factors.

  • EGFR Inaction vs Mutant
  • EGFR Inaction vs Mutant Ribbon
  • EGFR Inaction Ribbon
  • EGFR Mutant Ribbon


Inactive EGFR Tyrosine Kinase 3D Molecular Visualization

This 3D animation depicts EGFR bound by Erlotinib. Important protein structures like the alphaC-Helix, P-Loop and A-Loop are visualized to identify EGFR’s active state.

Epidermal growth factor receptor (EGFR) exists on the cell surface and is activated by binding of its specific ligands, including epidermal growth factor and transforming growth factor α (TGFα) (note, a full list of the ligands able to activate EGFR and other members of the ErbB family is given in the ErbB article). ErbB2 has no known direct activating ligand, and may be in an activated state constitutively or become active upon heterodimerization with other family members such as EGFR. Upon activation by its growth factor ligands, EGFR undergoes a transition from an inactive monomeric form to an active homodimer.


Mutations that lead to EGFR overexpression (known as upregulation) or overactivity have been associated with a number of cancers, including squamous-cell carcinoma of the lung (80% of cases), anal cancersglioblastoma (50%) and epithelian tumors of the head and neck (80-100%).[14] These somatic mutations involving EGFR lead to its constant activation, which produces uncontrolled cell division. In glioblastoma a more or less specific mutation of EGFR, called EGFRvIII is often observed.[16] Mutations, amplifications or misregulations of EGFR or family members are implicated in about 30% of all epithelial cancers

Active Mutant EGFR Tyrosine Kinase 3D Molecular Visualization

When EGFR proteins mutate, their A-loop change orientation and maintain an active position. This creates an open separation between the N and P lobes of the TK. In this conformation, the kinase maintains a favorable structure to promote continual tyrosine phosphorylation and uncontrolled cell division.

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If you’d like a desktop model of Active or Inactive EGFR, you can purchase one from our store. Prints available in multiple sizes.

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