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 language | English (US) |
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Pages (from-to) | 145-154 |
Number of pages | 10 |
Journal | FEBS Letters |
Volume | 415 |
Issue number | 2 |
DOIs | |
State | Published - Sep 29 1997 |
Externally published | Yes |
Keywords
- Chemical shift index
- Micelle
- Spin label
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology