Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins
Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K$^+$ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1991-12, Vol.254 (5037), p.1521-1523 |
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| creator | Bontems, Francois Roumestand, Christian Gilquin, Bernard Ménez, André Toma, Flavio |
| description | Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K$^+$ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel β sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern. |
| doi_str_mv | 10.1126/science.1720574 |
| format | Article |
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A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel β sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1720574</identifier><identifier>PMID: 1720574</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Society for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Blood Proteins - ultrastructure ; Cellular biology ; Charybdotoxin ; Consensus sequence ; Defensins ; Disulfides ; Hydrogen bonds ; Insect proteins ; Insects ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Neurotoxins - chemistry ; Nuclear magnetic resonance ; Poisoning ; Potassium Channels - drug effects ; Protein Conformation ; Protein folding ; Proteins ; Protons ; Scorpion Venoms - chemistry ; Scorpions ; Sequence Alignment ; Structural members ; Toxins ; Venom ; Venoms</subject><ispartof>Science (American Association for the Advancement of Science), 1991-12, Vol.254 (5037), p.1521-1523</ispartof><rights>Copyright 1991 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1991 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1991 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Dec 6, 1991</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c713t-ae839657eb99f22d9f6c3fa79c222119a0bb04db1f58ac8d1a9ab42a8cbf00d3</citedby><cites>FETCH-LOGICAL-c713t-ae839657eb99f22d9f6c3fa79c222119a0bb04db1f58ac8d1a9ab42a8cbf00d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2879446$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2879446$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1720574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bontems, Francois</creatorcontrib><creatorcontrib>Roumestand, Christian</creatorcontrib><creatorcontrib>Gilquin, Bernard</creatorcontrib><creatorcontrib>Ménez, André</creatorcontrib><creatorcontrib>Toma, Flavio</creatorcontrib><title>Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker of K$^+$ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel β sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Blood Proteins - ultrastructure</subject><subject>Cellular biology</subject><subject>Charybdotoxin</subject><subject>Consensus sequence</subject><subject>Defensins</subject><subject>Disulfides</subject><subject>Hydrogen bonds</subject><subject>Insect proteins</subject><subject>Insects</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Sequence Data</subject><subject>Neurotoxins - chemistry</subject><subject>Nuclear magnetic resonance</subject><subject>Poisoning</subject><subject>Potassium Channels - drug effects</subject><subject>Protein Conformation</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Protons</subject><subject>Scorpion Venoms - chemistry</subject><subject>Scorpions</subject><subject>Sequence 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three-dimensional structures of charybdotoxin (Chtx), a blocker of K$^+$ channels, have been previously reported. A high-resolution model depicting the tertiary structure of Chtx has been obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses a small triple-stranded antiparallel β sheet linked to a short helix by two disulfides and to an extended fragment by one disulfide, respectively. This motif also exists in all known structures of scorpion toxins, irrespective of their size, sequence, and function. Strikingly, antibacterial insect defensins also adopt this folding pattern.</abstract><cop>United States</cop><pub>American Society for the Advancement of Science</pub><pmid>1720574</pmid><doi>10.1126/science.1720574</doi><tpages>3</tpages></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1991-12, Vol.254 (5037), p.1521-1523 |
| issn | 0036-8075 1095-9203 |
| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Amino Acid Sequence Amino acids Animals Blood Proteins - ultrastructure Cellular biology Charybdotoxin Consensus sequence Defensins Disulfides Hydrogen bonds Insect proteins Insects Magnetic Resonance Spectroscopy Molecular Sequence Data Neurotoxins - chemistry Nuclear magnetic resonance Poisoning Potassium Channels - drug effects Protein Conformation Protein folding Proteins Protons Scorpion Venoms - chemistry Scorpions Sequence Alignment Structural members Toxins Venom Venoms |
| title | Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins |
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