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) |
|---|---|
| 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 |
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Keywords
- Chemical shift index
- Micelle
- Spin label
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
A cytoplasmic peptide of the neurotrophin receptor p75NTR : Induction of apoptosis and NMR determined helical conformation. / Hileman, Matthew R.; Chapman, Barbara S.; Rabizadeh, S.; Krishnan, Viswanathan V; Bredesen, Dale; Assa-Munt, Nuria; Plesniak, Leigh A.
In: FEBS Letters, Vol. 415, No. 2, 29.09.1997, p. 145-154.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A cytoplasmic peptide of the neurotrophin receptor p75NTR
T2 - Induction of apoptosis and NMR determined helical conformation
AU - Hileman, Matthew R.
AU - Chapman, Barbara S.
AU - Rabizadeh, S.
AU - Krishnan, Viswanathan V
AU - Bredesen, Dale
AU - Assa-Munt, Nuria
AU - Plesniak, Leigh A.
PY - 1997/9/29
Y1 - 1997/9/29
N2 - 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.
AB - 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.
KW - Chemical shift index
KW - Micelle
KW - Spin label
UR - http://www.scopus.com/inward/record.url?scp=0031590313&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031590313&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(97)01113-7
DO - 10.1016/S0014-5793(97)01113-7
M3 - Article
C2 - 9350985
AN - SCOPUS:0031590313
VL - 415
SP - 145
EP - 154
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -