Fig. 2.

Oncogenic extracellular domain mutations of ERBB2 reported in glioblastoma cause disulfide bond remodeling. (A) Model of the ERBB2 dimer made by superimposing the human [Protein Data Bank (PDB) ID code 2A91] and rat (PDB ID code 1N8Y) ERBB2 extracellular domain crystal structures onto an EGF-bound EGFR extracellular domain dimer crystal structure (PDB ID code 1IVO). Intramolecular disulfide bonds are indicated in green. (B) Immunoblot analysis of ERBB2 extracellular mutants reported in glioblastoma reveals formation of covalent dimers on nonreducing gels. pBp, pBabe puro vector; WT, wild-type ERBB2.