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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-6-6
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pubmed:abstractText |
Jingzhaotoxin-III (JZTX-III) is a peptide toxin isolated from the venom of the Chinese spider Chilobrachys jingzhao that inhibits Nav channels of rat cardiac myocytes by modifying voltage-dependent gating and also binds to Kv2.1 channel (Kd = 0.43 microM) with an action model similar to that of hanatoxin1 and SGTx1. The solution structure of JZTX-III was determined by (1)H 2D NMR method. The toxin adopts an ICK motif composed of three beta-strands connected by four turns. Structural comparison of JZTX-III with those of other ICK motif peptides shows that they all adopt a conserved surface profile, a hydrophobic patch surrounded by charged residues, which might be the crucial site for voltage-gating ion channel inhibition. Furthermore, the similar action model of JZTX-III affecting both Kv and Nav channels implies that JZTX-III recognized a conserved receptor within the voltage sensing domains, which is similar to that of hanatoxin1 binding to both Kv and Cav channels.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Kcnb1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Shab Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Spider Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/jingzhaotoxin-III, Chilobrachys...,
http://linkedlifedata.com/resource/pubmed/chemical/sodium channel protein type 5...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0041-0101
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
135-43
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pubmed:dateRevised |
2011-7-22
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pubmed:meshHeading |
pubmed-meshheading:17481690-Amino Acid Motifs,
pubmed-meshheading:17481690-Animals,
pubmed-meshheading:17481690-Arachnida,
pubmed-meshheading:17481690-Female,
pubmed-meshheading:17481690-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:17481690-Ion Channel Gating,
pubmed-meshheading:17481690-Models, Molecular,
pubmed-meshheading:17481690-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:17481690-Oocytes,
pubmed-meshheading:17481690-Peptides,
pubmed-meshheading:17481690-Potassium Channel Blockers,
pubmed-meshheading:17481690-Protein Conformation,
pubmed-meshheading:17481690-Rats,
pubmed-meshheading:17481690-Shab Potassium Channels,
pubmed-meshheading:17481690-Sodium Channel Blockers,
pubmed-meshheading:17481690-Sodium Channels,
pubmed-meshheading:17481690-Spider Venoms,
pubmed-meshheading:17481690-Structure-Activity Relationship,
pubmed-meshheading:17481690-Xenopus laevis
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pubmed:year |
2007
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pubmed:articleTitle |
Solution structure of Jingzhaotoxin-III, a peptide toxin inhibiting both Nav1.5 and Kv2.1 channels.
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pubmed:affiliation |
College of Life Sciences, Peking University, Beijing 100083, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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