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Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold
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| Zeitschriftentitel: | Bioscience Reports |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Bioscience Reports, 33, 2013, 3 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
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| Schlagwörter: |
| author_facet |
Gao, Bin Harvey, Peta J. Craik, David J. Ronjat, Michel De Waard, Michel Zhu, Shunyi Gao, Bin Harvey, Peta J. Craik, David J. Ronjat, Michel De Waard, Michel Zhu, Shunyi |
|---|---|
| author |
Gao, Bin Harvey, Peta J. Craik, David J. Ronjat, Michel De Waard, Michel Zhu, Shunyi |
| spellingShingle |
Gao, Bin Harvey, Peta J. Craik, David J. Ronjat, Michel De Waard, Michel Zhu, Shunyi Bioscience Reports Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold Cell Biology Molecular Biology Biochemistry Biophysics |
| author_sort |
gao, bin |
| spelling |
Gao, Bin Harvey, Peta J. Craik, David J. Ronjat, Michel De Waard, Michel Zhu, Shunyi 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20130052 <jats:p>The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new scorpion venom-derived K+ channel toxin (named λ-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. λ-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel β-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels/ryanodine receptors, which is remarkably different from the previously known scorpion venom ICK peptides. The removal of two C-terminal residues of λ-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of λ-MeuKTx-1. The presence of a functional dyad in λ-MeuKTx-1 supports functional convergence among scorpion venom peptides with different folds. Furthermore, similarities in precursor organization, exon–intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first scorpion venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin.</jats:p> Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold Bioscience Reports |
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| title |
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_unstemmed |
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_full |
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_fullStr |
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_full_unstemmed |
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_short |
Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_sort |
functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| topic |
Cell Biology Molecular Biology Biochemistry Biophysics |
| url |
http://dx.doi.org/10.1042/bsr20130052 |
| publishDate |
2013 |
| physical |
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| description |
<jats:p>The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new scorpion venom-derived K+ channel toxin (named λ-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. λ-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel β-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels/ryanodine receptors, which is remarkably different from the previously known scorpion venom ICK peptides. The removal of two C-terminal residues of λ-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of λ-MeuKTx-1. The presence of a functional dyad in λ-MeuKTx-1 supports functional convergence among scorpion venom peptides with different folds. Furthermore, similarities in precursor organization, exon–intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first scorpion venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin.</jats:p> |
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| author | Gao, Bin, Harvey, Peta J., Craik, David J., Ronjat, Michel, De Waard, Michel, Zhu, Shunyi |
| author_facet | Gao, Bin, Harvey, Peta J., Craik, David J., Ronjat, Michel, De Waard, Michel, Zhu, Shunyi, Gao, Bin, Harvey, Peta J., Craik, David J., Ronjat, Michel, De Waard, Michel, Zhu, Shunyi |
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| description | <jats:p>The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new scorpion venom-derived K+ channel toxin (named λ-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. λ-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel β-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels/ryanodine receptors, which is remarkably different from the previously known scorpion venom ICK peptides. The removal of two C-terminal residues of λ-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of λ-MeuKTx-1. The presence of a functional dyad in λ-MeuKTx-1 supports functional convergence among scorpion venom peptides with different folds. Furthermore, similarities in precursor organization, exon–intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first scorpion venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin.</jats:p> |
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| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
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| spelling | Gao, Bin Harvey, Peta J. Craik, David J. Ronjat, Michel De Waard, Michel Zhu, Shunyi 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20130052 <jats:p>The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new scorpion venom-derived K+ channel toxin (named λ-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. λ-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel β-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels/ryanodine receptors, which is remarkably different from the previously known scorpion venom ICK peptides. The removal of two C-terminal residues of λ-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of λ-MeuKTx-1. The presence of a functional dyad in λ-MeuKTx-1 supports functional convergence among scorpion venom peptides with different folds. Furthermore, similarities in precursor organization, exon–intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first scorpion venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin.</jats:p> Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold Bioscience Reports |
| spellingShingle | Gao, Bin, Harvey, Peta J., Craik, David J., Ronjat, Michel, De Waard, Michel, Zhu, Shunyi, Bioscience Reports, Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold, Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| title | Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_full | Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_fullStr | Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_full_unstemmed | Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_short | Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_sort | functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| title_unstemmed | Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold |
| topic | Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| url | http://dx.doi.org/10.1042/bsr20130052 |