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1q2k
From Proteopedia
(New page: 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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| - | [[Image:1q2k.jpg|left|200px]]<br /><applet load="1q2k" size=" | + | [[Image:1q2k.jpg|left|200px]]<br /><applet load="1q2k" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q2k" /> | caption="1q2k" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Chi, C W.]] |
[[Category: Lu, W.]] | [[Category: Lu, W.]] | ||
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
| Line 22: | Line 22: | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:10 2008'' |
Revision as of 12:35, 21 February 2008
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Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch
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.
About this Structure
1Q2K is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:35:10 2008
Categories: Single protein | Cai, Z. | Chi, C W. | Lu, W. | Shi, Y. | Wu, J. | Xu, C. | Xu, Y. | Alpha-helix | Beta-sheet
