Structural basis for a functional antagonist in the transforming growth factor β superfamily

Robert W. Cook, Thomas B. Thompson, Sudhi P. Kurup, Theodore S. Jardetzky, Teresa K. Woodruff*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Within the transforming growth factor β superfamily, the agonist-antagonist relationship between activin and inhibin is unique and critical to integrated reproductive function. Activin acts in the pituitary to stimulate follicle-stimulating hormone, and is antagonized by endocrine acting, gonadally derived inhibin. We have undertaken a mutational analysis of the activin βA subunit to determine the precise structural aspects that contribute to inhibin antagonism of activin. By substituting specific amino acid residues in the activin βA subunit with similarly aligned amino acids from the α subunit, we have pinpointed the residues required for activin receptor binding and activity, as well as for inhibin antagonism of activin through its receptors. Additionally, we have identified an activin mutant with a higher affinity for the activin type I receptor that provides structural evidence for the evolution of ligand-receptor interactions within the transforming growth factor β superfamily.

Original languageEnglish (US)
Pages (from-to)40177-40186
Number of pages10
JournalJournal of Biological Chemistry
Issue number48
StatePublished - Dec 2 2005

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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