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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'''3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES'''<br />
'''3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1KCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_purpurascens Conus purpurascens] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KCP OCA].
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1KCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_purpurascens Conus purpurascens] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCP OCA].
==Reference==
==Reference==
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[[Category: potassium channel inhibitor]]
[[Category: potassium channel inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:03:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:35 2008''

Revision as of 11:32, 21 February 2008


1kcp

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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 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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