Solution structure of a defensin-like peptide from platypus venom

Allan M. Torres; Xiuhong Wang; Jamie I. Fletcher; Dianne Alewood; Paul F. Alewood; Ross Smith; Richard J. Simpson; Graham M. Nicholson; Struan K. Sutherland; Cliff H. Gallagher; Glenn F. King; Philip W. Kuchel

doi:10.1042/0264-6021:3410785

Solution structure of a defensin-like peptide from platypus venom

Allan M. Torres, Xiuhong Wang, Jamie I. Fletcher, Dianne Alewood, Paul F. Alewood, Ross Smith, Richard J. Simpson, Graham M. Nicholson, Struan K. Sutherland, Cliff H. Gallagher, Glenn F. King, Philip W. Kuchel

Research output: Contribution to journal › Article › peer-review

58 Citations (Scopus)

Abstract

Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-sheet comprising residues 15-18 and 37-40 and a small 3₁₀ helix spanning residues 10-12. The overall three-dimensional fold is similar to that of β-defensin-12, and similar to the sodium channel neurotoxin ShI (Stichodactyla helianthus neurotoxin I). However, the side chains known to be functionally important in β-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents.

Original language	English
Pages (from-to)	785-794
Number of pages	10
Journal	The Biochemical Journal
Volume	341
Issue number	3
DOIs	https://doi.org/10.1042/0264-6021:3410785
Publication status	Published - 1 Aug 1999
Externally published	Yes

Keywords

β-defensin fold
HPLC separation of venom components
NMR of proteins
Platypus toxins
Protein folding

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10.1042/0264-6021:3410785

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title = "Solution structure of a defensin-like peptide from platypus venom",

abstract = "Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-sheet comprising residues 15-18 and 37-40 and a small 310 helix spanning residues 10-12. The overall three-dimensional fold is similar to that of β-defensin-12, and similar to the sodium channel neurotoxin ShI (Stichodactyla helianthus neurotoxin I). However, the side chains known to be functionally important in β-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents.",

keywords = "β-defensin fold, HPLC separation of venom components, NMR of proteins, Platypus toxins, Protein folding",

author = "Torres, {Allan M.} and Xiuhong Wang and Fletcher, {Jamie I.} and Dianne Alewood and Alewood, {Paul F.} and Ross Smith and Simpson, {Richard J.} and Nicholson, {Graham M.} and Sutherland, {Struan K.} and Gallagher, {Cliff H.} and King, {Glenn F.} and Kuchel, {Philip W.}",

year = "1999",

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doi = "10.1042/0264-6021:3410785",

language = "English",

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T1 - Solution structure of a defensin-like peptide from platypus venom

AU - Torres, Allan M.

AU - Wang, Xiuhong

AU - Fletcher, Jamie I.

AU - Alewood, Dianne

AU - Alewood, Paul F.

AU - Smith, Ross

AU - Simpson, Richard J.

AU - Nicholson, Graham M.

AU - Sutherland, Struan K.

AU - Gallagher, Cliff H.

AU - King, Glenn F.

AU - Kuchel, Philip W.

PY - 1999/8/1

Y1 - 1999/8/1

N2 - Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-sheet comprising residues 15-18 and 37-40 and a small 310 helix spanning residues 10-12. The overall three-dimensional fold is similar to that of β-defensin-12, and similar to the sodium channel neurotoxin ShI (Stichodactyla helianthus neurotoxin I). However, the side chains known to be functionally important in β-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents.

AB - Three defensin-like peptides (DLPs) were isolated from platypus venom and sequenced. One of these peptides, DLP-1, was synthesized chemically and its three-dimensional structure was determined using NMR spectroscopy. The main structural elements of this 42-residue peptide were an anti-parallel β-sheet comprising residues 15-18 and 37-40 and a small 310 helix spanning residues 10-12. The overall three-dimensional fold is similar to that of β-defensin-12, and similar to the sodium channel neurotoxin ShI (Stichodactyla helianthus neurotoxin I). However, the side chains known to be functionally important in β-defensin-12 and ShI are not conserved in DLP-1, suggesting that it has a different biological function. Consistent with this contention, we showed that DLP-1 possesses no anti-microbial properties and has no observable activity on rat dorsal-root-ganglion sodium-channel currents.

KW - β-defensin fold

KW - HPLC separation of venom components

KW - NMR of proteins

KW - Platypus toxins

KW - Protein folding

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ER -

Solution structure of a defensin-like peptide from platypus venom

Abstract

Keywords

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