Disulfide bond structure of human epidermal growth factor receptor

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

研究成果: ジャーナルへの寄稿学術誌査読

74 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)11150-11157
ページ数8
ジャーナルJournal of Biological Chemistry
273
18
DOI
出版ステータス出版済み - 5月 1 1998
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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