A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding

Hiroshi Koide, Yutaka Muto, Hidefumi Kasai, Kaoru Kohri, Kumiko Hoshi, Seizo Takahashi, Ken ichi Tsukumo, Tetsuyuki Sasaki, Takanori Oka, Tetsuo Miyake, Tohru Fuwa, Daisuke Kohda, Fuyuhiko Inagaki, Tatsuo Miyazawa, Shigeyuki Yokoyama

研究成果: Article査読

22 被引用数 (Scopus)

抄録

The isoleucine-23 residue of human epidermal growth factor (hEGF) was substituted by a variety of amino acid residues and the receptor-binding activities of variant hEGFs were determined by the use of human KB cell. Tight receptor binding was found of variants with hydrophobic amino acid residues in position 23. The size of the isoleucine residue was nearly optimum for the receptor binding as compared with other hydrophobic residues. The structure analysis by two-dimensional nuclear magnetic resonance spectroscopy showed that the substitution at position 23 only slightly affected the tertiary structure of hEGF. These indicate that the side chain of isoleucine residue in position 23, which is exposed on the protein surface, directly binds to a hydrophobic pocket of the receptor.

本文言語English
ページ(範囲)257-261
ページ数5
ジャーナルBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
1120
3
DOI
出版ステータスPublished - 1992 4月 17
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

フィンガープリント

「A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding」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