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J. Biochem, 1988, Vol. 103, No. 5 741-743
© 1988 Japanese Biochemical Society

other

Tertiary Structure of Mouse Epidermal Growth Factor Determined by Two-Dimensional 1H NMR

Daisuke Kohda, Faculty of Science*, Nobuhiro Go**, Kyozo Hayashi*** and Fuyuhiko Inagaki*

* Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science Bunkyo-ku, Tokyo 113
** Department of Chemistry, Kyoto University Sakyo-ku, Kyoto, Kyoto 606
*** Department of Pharmaceutics, Gifu Pharmaceutical University Gifu, Gifu 502

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.


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