Disulfide bond structure of human epidermal growth factor receptor

Yoshito Abe, Masafumi Odaka, Fuyuhiko Inagaki, Irit Lax, Joseph Schlessinger, Daisuke Kohda

Research output: Contribution to journalArticlepeer-review

75 Citations (Scopus)


The extracellular domain of the human epidermal growth factor receptor (sEGFR) consists of 621 amino acid residues, including 50 cysteines. The connections of the 25 disulfide bonds in the recombinant sEGFR protein, obtained from Chinese hamster ovary cells, have been determined using N- terminal sequencing and matrix-assisted laser desorption/ionization mass spectroscopy. We identified a basic repeat of eight cysteines with a 1-3, 2- 4, 5-6, and 7-8 disulfide pairing pattern in the two cysteine-rich regions of sEGFR. By comparison to other cysteine-rich motifs, it was concluded that the cysteine-rich repeat of sEGFR belongs to the laminin-type EGR-like (LE) structural motif. Three-dimensional structure models of the two cysteine- rich regions have been built, based on the three-dimensional structures of the LE domains from the laminin γ1 chain and secondary structure predictions for the EGF receptor.

Original languageEnglish
Pages (from-to)11150-11157
Number of pages8
JournalJournal of Biological Chemistry
Issue number18
Publication statusPublished - May 1 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Disulfide bond structure of human epidermal growth factor receptor'. Together they form a unique fingerprint.

Cite this