1kcp
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(New page: 200px<br /><applet load="1kcp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kcp" /> '''3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL P...)
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Revision as of 16:56, 20 November 2007
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3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES
Overview
kappa-Conotoxin PVIIA from the venom of Conus purpurascens is the first, cone snail toxin that was described to block potassium channels. We, synthesized chemically this toxin and showed that its disulfide bridge, pattern is similar to those of omega- and delta-conotoxins., kappa-conotoxin competes with radioactive alpha-dendrotoxin for binding to, rat brain synaptosomes, confirming its capacity to bind to potassium, channels; however, it behaves as a weak competitor. The three-dimensional, structure of kappa-conotoxin PVIIA, as elucidated by NMR spectroscopy and, molecular modeling, comprises two large parallel loops stabilized by a, triple-stranded antiparallel beta-sheet and three disulfide bridges. The, overall fold of kappa-conotoxin is similar to that of calcium, channel-blocking omega-conotoxins but differs from those of potassium, channel-blocking toxins from sea anemones, scorpions, and snakes. Local, topographies of kappa-conotoxin PVIIA that might account for its capacity, to recognize Kv1-type potassium channels are discussed.
About this Structure
1KCP is a Single protein structure of sequence from Conus purpurascens with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails., Savarin P, Guenneugues M, Gilquin B, Lamthanh H, Gasparini S, Zinn-Justin S, Menez A, Biochemistry. 1998 Apr 21;37(16):5407-16. PMID:9548922
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