A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor

D. Kohda, M. Odaka, I. Lax, H. Kawasaki, K. Suzuki, A. Ullrich, J. Schlessinger, F. Inagaki

研究成果: ジャーナルへの寄稿記事

42 引用 (Scopus)

抄録

Elucidation of the three-dimensional structure of the complex of the epidermal growth factor (EGF) and its receptor is essential for understanding the molecular mechanisms of the EGF-receptor interaction and EGF-induced receptor-receptor interaction. NMR is useful to investigate interactions in solution between macromolecules at atomic resolution, but has a limitation in molecular masses of target proteins: less than 300 residues. We have prepared a fragment with apparent molecular mass of 40 kDa in SDS gels from the soluble extracellular domain of the EGF receptor (sEGFR, 619 residues) by sequential limited proteolysis with proteinase K and bromelain. This fragment is a monomeric structural domain consisting of 202 amino acid residues (Cys302-Arg503) and 18-kDa sugar chains, and binds EGF and transforming growth factor-α (TGFα). This 40-kDa domain has a dissociation constant of about 1 μM for human TGFα, which is similar to that of the parental sEGFR. sEGFR oligomerizes in response to EGF and TGFα, while the 40-kDa domain does not, suggesting that the sequences other than this domain is required for receptor oligomerization. The 40-kDa ligand-binding domain described in this report is suitable for analysis by various physico-chemical approaches such as NMR.

元の言語英語
ページ(範囲)1976-1981
ページ数6
ジャーナルJournal of Biological Chemistry
268
発行部数3
出版物ステータス出版済み - 1 1 1993
外部発表Yes

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Proteolysis
Transforming Growth Factors
Epidermal Growth Factor Receptor
Epidermal Growth Factor
Molecular mass
Nuclear magnetic resonance
Bromelains
Endopeptidase K
Oligomerization
Macromolecules
Sugars
Gels
Ligands
Amino Acids
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. / Kohda, D.; Odaka, M.; Lax, I.; Kawasaki, H.; Suzuki, K.; Ullrich, A.; Schlessinger, J.; Inagaki, F.

:: Journal of Biological Chemistry, 巻 268, 番号 3, 01.01.1993, p. 1976-1981.

研究成果: ジャーナルへの寄稿記事

Kohda, D. ; Odaka, M. ; Lax, I. ; Kawasaki, H. ; Suzuki, K. ; Ullrich, A. ; Schlessinger, J. ; Inagaki, F. / A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. :: Journal of Biological Chemistry. 1993 ; 巻 268, 番号 3. pp. 1976-1981.
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T1 - A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor

AU - Kohda, D.

AU - Odaka, M.

AU - Lax, I.

AU - Kawasaki, H.

AU - Suzuki, K.

AU - Ullrich, A.

AU - Schlessinger, J.

AU - Inagaki, F.

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