Solution structure of betacellulin, a new member of EGF-family ligands

Kazunori Miura, Hideki Doura, Tomoyasu Aizawa, Hiroko Tada, Masaharu Seno, Hidenori Yamada, Keiichi Kawanob

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


The solution structure of the EGF-like domain of betacellulin (BTCe), a newly discovered member of the epidermal growth factor (EGF) family, has been determined using two-dimensional nuclear magnetic resonance spectroscopy. This is the first report to identify the solution structure of the EGF-family ligand monomers that interact with both ErbB-1 and ErbB-4. The solution structure of BTCe was calculated using 538 NMR-derived restraints. The overall structure of BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds. It appears that BTCe is comprised of five β-strands and one short 310 helical turn. The secondary structural elements of BTCe are basically similar to those of the other EGF-family proteins, except that several significant variations of the structural properties were found. It is suggested that the structural variations between BTCe and the other EGF-family ligands may affect the specific receptor-recognition properties of EGF-family ligands.

Original languageEnglish
Pages (from-to)1040-1046
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number5
Publication statusPublished - 2002
Externally publishedYes


  • Betacellulin
  • Epidermal growth factor family
  • Nuclear magnetic resonance
  • Solution structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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