1q2k: Difference between revisions

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New page: left|200px<br /><applet load="1q2k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q2k" /> '''Solution structure of BmBKTx1 a new potassiu...
 
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'''Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch'''<br />
'''Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1Q2K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA].  
1Q2K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q2K OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cai, Z.]]
[[Category: Cai, Z.]]
[[Category: Chi, C.W.]]
[[Category: Chi, C W.]]
[[Category: Lu, W.]]
[[Category: Lu, W.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: beta-sheet]]
[[Category: beta-sheet]]


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Revision as of 15:35, 21 February 2008

File:1q2k.jpg


1q2k

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Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch

OverviewOverview

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.

About this StructureAbout this Structure

1Q2K is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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

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