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 journalArticlepeer-review

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 - May 1988
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Tertiary structure of mouse epidermal growth factor determined by two-dimensional <sup>1</sup>H NMR'. Together they form a unique fingerprint.

Cite this