1q2k
From Proteopedia
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| - | [[Image:1q2k.jpg|left|200px]] | + | [[Image:1q2k.jpg|left|200px]] |
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| - | '''Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch''' | + | {{Structure |
| + | |PDB= 1q2k |SIZE=350|CAPTION= <scene name='initialview01'>1q2k</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q2K is a [ | + | 1Q2K is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15049683 15049683] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cai, Z.]] | [[Category: Cai, Z.]] | ||
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[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:32:09 2008'' |
Revision as of 11:32, 20 March 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 Mar 20 13:32:09 2008
Categories: Single protein | Cai, Z. | Chi, C W. | Lu, W. | Shi, Y. | Wu, J. | Xu, C. | Xu, Y. | Alpha-helix | Beta-sheet
