Recognition of an antiparallel β-sheet structure of human epidermal growth factor by its receptor Site-directed mutagenesis studies of Ala-30 and Asn-32

Hiroshi Koide, Yutaka Muto, Hidefumi Kasai, Kumiko Hoshi, Hiromi Takusari, Kaoru Kohri, Seizo Takahashi, Tetsuyuki Sasaki, Ken ichi Tsukumo, Tetsuo Miyake, Tohru Fuwa, Tatsuo Miyazawa, Shigeyuki Yokoyama

研究成果: Article査読

9 被引用数 (Scopus)

抄録

The Ala-30 and Asn-32 residues involved in the major antiparallel β-sheet structure of human epidermal growth factor (hEGF) were substituted with various amino acid residues, and the receptor-binding affinities of the nine variant hEGFs were determined by the use of human KB cells. The Ala-30→Arg. Ala-30→His and Ala-30→Phe substitutions drastically reduced the binding affinity, suggesting that the side chain in position 30 of Ala-30 of hEGF is required to be small for the receptor binding. The Asn-32→Asp substitution significantly reduced the binding affinity, while the Asn-32→His variant could bind to the receptor as well as to the wild-type hEGF. Therefore, it seems to be important for receptor binding that the side chain in position 32 does not have a negative charve but does have an NH group. Thus, we propose that, in the ligand-receptor complex, the receptor recognizes, on one side of the antiparallel β-sheet structure of hEGF, a wider contact area than previously suggested.

本文言語English
ページ(範囲)39-42
ページ数4
ジャーナルFEBS Letters
302
1
DOI
出版ステータスPublished - 1992 5月 4
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

フィンガープリント

「Recognition of an antiparallel β-sheet structure of human epidermal growth factor by its receptor Site-directed mutagenesis studies of Ala-30 and Asn-32」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル