Tertiary structure of mouse epidermal growth factor determined by two-dimensional 1H NMR

Daisuke Kohda, Nobuhiro Go, Kyozo Hayashi, Fuyuhiko Inagaki

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

The tertiary structure of mouse epidermal growth factor (EGF) in solution (28°C, pH 2.0) was studied by two-dimensional NMR spectroscopy. Proton-proton distance constraints derived from NOESY spectra were used to construct a mechanical molecular model of mouse EGF, which was subsequently checked by means of a preliminary distance geometry calculation. The chain-folds in the two structural domains of mouse EGF were very similar to those previously reported (Montelione et al. (1987) Proc. Natl. Acad. Sci. U.S. 84, 5226-5230). However, the relative orientations of the two domains were different. Because we could assign much more inter-domain NOEs, the relative orientations of the two domains were well determined in our model. The hollow between the two domains may function as a binding site for the EGF receptor.

Original languageEnglish
Pages (from-to)741-743
Number of pages3
JournalJournal of biochemistry
Volume103
Issue number5
DOIs
Publication statusPublished - Jan 1 1988
Externally publishedYes

Fingerprint

Epidermal Growth Factor
Nuclear magnetic resonance
Protons
Molecular Models
Epidermal Growth Factor Receptor
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Binding Sites
Geometry
Proton Magnetic Resonance Spectroscopy

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Tertiary structure of mouse epidermal growth factor determined by two-dimensional 1H NMR. / Kohda, Daisuke; Go, Nobuhiro; Hayashi, Kyozo; Inagaki, Fuyuhiko.

In: Journal of biochemistry, Vol. 103, No. 5, 01.01.1988, p. 741-743.

Research output: Contribution to journalArticle

Kohda, Daisuke ; Go, Nobuhiro ; Hayashi, Kyozo ; Inagaki, Fuyuhiko. / Tertiary structure of mouse epidermal growth factor determined by two-dimensional 1H NMR. In: Journal of biochemistry. 1988 ; Vol. 103, No. 5. pp. 741-743.
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