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

doi:10.1016/0167-4838(92)90245-9

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 journal › Article › peer-review

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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 language	English
Pages (from-to)	257-261
Number of pages	5
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1120
Issue number	3
DOIs	https://doi.org/10.1016/0167-4838(92)90245-9
Publication status	Published - Apr 17 1992
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology

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10.1016/0167-4838(92)90245-9

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Koide, H., Muto, Y., Kasai, H., Kohri, K., Hoshi, K., Takahashi, S., Tsukumo, K. I., 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 - Protein Structure and Molecular Enzymology, 1120(3), 257-261. https://doi.org/10.1016/0167-4838(92)90245-9

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 - Protein Structure and Molecular Enzymology, vol. 1120, no. 3, pp. 257-261. https://doi.org/10.1016/0167-4838(92)90245-9

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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",

note = "Funding Information: This work was supported in part by Grant-in-Aid 02250106 foSrc ientificR esearchi n Priority Areas from the Ministry of Education, Science and Culture of Japan.",

year = "1992",

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doi = "10.1016/0167-4838(92)90245-9",

language = "English",

volume = "1120",

pages = "257--261",

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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

N1 - Funding Information: This work was supported in part by Grant-in-Aid 02250106 foSrc ientificR esearchi n Priority Areas from the Ministry of Education, Science and Culture of Japan.

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.

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ER -

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

Abstract

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