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==Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch== | |||
<StructureSection load='1q2k' size='340' side='right' caption='[[1q2k]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1q2k]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q2K FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q2k RCSB], [http://www.ebi.ac.uk/pdbsum/1q2k PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed. | |||
Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683<ref>PMID:15049683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Potassium channel toxin|Potassium channel toxin]] | *[[Potassium channel toxin|Potassium channel toxin]] | ||
[[Category: Cai, Z | == References == | ||
[[Category: Chi, C W | <references/> | ||
[[Category: Lu, W | __TOC__ | ||
[[Category: Shi, Y | </StructureSection> | ||
[[Category: Wu, J | [[Category: Cai, Z]] | ||
[[Category: Xu, C | [[Category: Chi, C W]] | ||
[[Category: Xu, Y | [[Category: Lu, W]] | ||
[[Category: Shi, Y]] | |||
[[Category: Wu, J]] | |||
[[Category: Xu, C]] | |||
[[Category: Xu, Y]] | |||
[[Category: Alpha-helix]] | [[Category: Alpha-helix]] | ||
[[Category: Beta-sheet]] | [[Category: Beta-sheet]] | ||
[[Category: Toxin]] | [[Category: Toxin]] | ||
Revision as of 17:16, 17 December 2014
Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi KarschSolution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch
Structural highlights
Publication Abstract from PubMedBmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed. Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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