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

doi:10.1016/S0014-5793(97)01113-7

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 journal › Article › peer-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 language	English (US)
Pages (from-to)	145-154
Number of pages	10
Journal	FEBS Letters
Volume	415
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(97)01113-7
State	Published - Sep 29 1997
Externally published	Yes

Keywords

Chemical shift index
Micelle
Spin label

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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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 › peer-review

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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.",

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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.

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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.

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

Abstract

Keywords

ASJC Scopus subject areas

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