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From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/STXA_SYNHO STXA_SYNHO]] This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref> [[http://www.uniprot.org/uniprot/STXB_SYNHO STXB_SYNHO]] This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref> | [[http://www.uniprot.org/uniprot/STXA_SYNHO STXA_SYNHO]] This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref> [[http://www.uniprot.org/uniprot/STXB_SYNHO STXB_SYNHO]] This lethal (towards mice) toxin induces hemolytic activities due to its ability to form pores in the cell membrane, elicits potent hypotension which is endothelium-dependent and appears to be mediated by the nitric oxide pathway and activation of potassium channels, displays edema-inducing activities, increases vascular permeability, induces endothelium-dependent vasorelaxation of isolated rat aorta, induces platelet aggregation, is myotoxic and interferes irreversibly with neuromuscular function.<ref>PMID:1790672</ref> <ref>PMID:8079369</ref> <ref>PMID:9271089</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The lethal factor in stonefish venom is stonustoxin (SNTX), a heterodimeric cytolytic protein that induces cardiovascular collapse in humans and native predators. Here, using X-ray crystallography, we make the unexpected finding that SNTX is a pore-forming member of an ancient branch of the Membrane Attack Complex-Perforin/Cholesterol-Dependent Cytolysin (MACPF/CDC) superfamily. SNTX comprises two homologous subunits (alpha and beta), each of which comprises an N-terminal pore-forming MACPF/CDC domain, a central focal adhesion-targeting domain, a thioredoxin domain, and a C-terminal tripartite motif family-like PRY SPla and the RYanodine Receptor immune recognition domain. Crucially, the structure reveals that the two MACPF domains are in complex with one another and arranged into a stable early prepore-like assembly. These data provide long sought after near-atomic resolution insights into how MACPF/CDC proteins assemble into prepores on the surface of membranes. Furthermore, our analyses reveal that SNTX-like MACPF/CDCs are distributed throughout eukaryotic life and play a broader, possibly immune-related function outside venom. | ||
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| + | Stonefish toxin defines an ancient branch of the perforin-like superfamily.,Ellisdon AM, Reboul CF, Panjikar S, Huynh K, Oellig CA, Winter KL, Dunstone MA, Hodgson WC, Seymour J, Dearden PK, Tweten RK, Whisstock JC, McGowan S Proc Natl Acad Sci U S A. 2015 Dec 1. pii: 201507622. PMID:26627714<ref>PMID:26627714</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4wvm" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:05, 16 December 2015
Stonustoxin structure
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