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

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)257-261
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1120
Issue number3
DOIs
Publication statusPublished - Apr 17 1992

Fingerprint

Mutagenesis
Isoleucine
Site-Directed Mutagenesis
Epidermal Growth Factor Receptor
Epidermal Growth Factor
Amino Acid Receptors
KB Cells
Amino Acids
Nuclear magnetic resonance spectroscopy
Membrane Proteins
Substitution reactions
Magnetic Resonance Spectroscopy

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding. / Koide, Hiroshi; Muto, Yutaka; Kasai, Hidefumi; Kohri, Kaoru; Hoshi, Kumiko; Takahashi, Seizo; Tsukumo, Ken ichi; Sasaki, Tetsuyuki; Oka, Takanori; Miyake, Tetsuo; Fuwa, Tohru; Kohda, Daisuke; Inagaki, Fuyuhiko; Miyazawa, Tatsuo; Yokoyama, Shigeyuki.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1120, No. 3, 17.04.1992, p. 257-261.

Research output: Contribution to journalArticle

Koide, H, Muto, Y, Kasai, H, Kohri, K, Hoshi, K, Takahashi, S, Tsukumo, KI, Sasaki, T, Oka, T, Miyake, T, Fuwa, T, Kohda, D, Inagaki, F, Miyazawa, T & Yokoyama, S 1992, 'A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding', Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, vol. 1120, no. 3, pp. 257-261. https://doi.org/10.1016/0167-4838(92)90245-9
Koide, Hiroshi ; Muto, Yutaka ; Kasai, Hidefumi ; Kohri, Kaoru ; Hoshi, Kumiko ; Takahashi, Seizo ; Tsukumo, Ken ichi ; Sasaki, Tetsuyuki ; Oka, Takanori ; Miyake, Tetsuo ; Fuwa, Tohru ; Kohda, Daisuke ; Inagaki, Fuyuhiko ; Miyazawa, Tatsuo ; Yokoyama, Shigeyuki. / A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding. In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular. 1992 ; Vol. 1120, No. 3. pp. 257-261.
@article{9a13ffdbb7c0446c962e246712a751ef,
title = "A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding",
abstract = "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.",
author = "Hiroshi Koide and Yutaka Muto and Hidefumi Kasai and Kaoru Kohri and Kumiko Hoshi and Seizo Takahashi and Tsukumo, {Ken ichi} and Tetsuyuki Sasaki and Takanori Oka and Tetsuo Miyake and Tohru Fuwa and Daisuke Kohda and Fuyuhiko Inagaki and Tatsuo Miyazawa and Shigeyuki Yokoyama",
year = "1992",
month = "4",
day = "17",
doi = "10.1016/0167-4838(92)90245-9",
language = "English",
volume = "1120",
pages = "257--261",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - A site-directed mutagenesis study on the role of isoleucine-23 of human epidermal growth factor in the receptor binding

AU - Koide, Hiroshi

AU - Muto, Yutaka

AU - Kasai, Hidefumi

AU - Kohri, Kaoru

AU - Hoshi, Kumiko

AU - Takahashi, Seizo

AU - Tsukumo, Ken ichi

AU - Sasaki, Tetsuyuki

AU - Oka, Takanori

AU - Miyake, Tetsuo

AU - Fuwa, Tohru

AU - Kohda, Daisuke

AU - Inagaki, Fuyuhiko

AU - Miyazawa, Tatsuo

AU - Yokoyama, Shigeyuki

PY - 1992/4/17

Y1 - 1992/4/17

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0026518978&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026518978&partnerID=8YFLogxK

U2 - 10.1016/0167-4838(92)90245-9

DO - 10.1016/0167-4838(92)90245-9

M3 - Article

C2 - 1576151

AN - SCOPUS:0026518978

VL - 1120

SP - 257

EP - 261

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 3

ER -