A cytoplasmic peptide of the neurotrophin receptor p75NTR: Induction of apoptosis and NMR determined helical conformation

Matthew R. Hileman, Barbara S. Chapman, S. Rabizadeh, Viswanathan V Krishnan, Dale Bredesen, Nuria Assa-Munt, Leigh A. Plesniak

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The neurotrophin receptor (NTR) and tumor necrosis factor receptor family of receptors regulate apoptotic cell death during development and in adult tissues [Beutler and van Huffel, Science 264 (1994) 667-668]. We have examined a fragment of p75NTR from the carboxyl terminus of the receptor and a variant form of this peptide via NMR techniques and in vitro assays for apoptotic activity. The wild type peptide induces apoptosis and adopts a helical conformation oriented parallel to the surface of lipid micelles, whereas the variant form adopts a non-helical conformation in the presence of lipid and shows no activity. These experiments suggest a link between structure and function of the two peptides.

Original languageEnglish (US)
Pages (from-to)145-154
Number of pages10
JournalFEBS Letters
Volume415
Issue number2
DOIs
StatePublished - Sep 29 1997
Externally publishedYes

Keywords

  • Chemical shift index
  • Micelle
  • Spin label

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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