1m2s
From Proteopedia
(New page: 200px<br /><applet load="1m2s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m2s" /> '''Solution Structure of A New Potassium Channe...) |
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| - | [[Image:1m2s.gif|left|200px]]<br /><applet load="1m2s" size=" | + | [[Image:1m2s.gif|left|200px]]<br /><applet load="1m2s" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of A New Potassium Channels Blocker from the Venom of Chinese Scorpion Buthus martensi Karsch'''<br /> | '''Solution Structure of A New Potassium Channels Blocker from the Venom of Chinese Scorpion Buthus martensi Karsch'''<br /> | ||
==Overview== | ==Overview== | ||
| - | This article reports the solution structure of BmTx3B (alpha-KTx16.2), a | + | This article reports the solution structure of BmTx3B (alpha-KTx16.2), a potassium channel blocker belonging to the subfamily alpha-KTx16, purified from the venom of the Chinese scorpion Buthus martensi Karsch. In solution, BmTx3B assumes a typical CSalphabeta motif, with an alpha-helix connected to a triple-stranded beta-sheet by 3 disulfide bridges, which belongs to the first structural group of short-chain scorpion toxins. On the other hand, BmTx3B is quite different from other toxins (such as ChTx and AgTx2) of this group in terms of the electrostatic and hydrophobic surface distribution. The functional surface (beta-face) of the molecule is characterized by less basic residues (only 2: Lys28 and Arg35) and extra aromatic residues (Phe1, Phe9, Trp15, and Tyr37). The peptide shows a great preference for the Kca1.1 channel over the Kv channel (about a 10(3)-fold difference). The model of BmTx3B/Kca1.1 channel complex generated by docking and dynamic simulation reveals that the stable binding between the BmTx3B and Kca1.1 channel is favored by a number of aromatic pi-pi stacking interactions. The influences of these structural features on the kinetic behavior of the toxin binding to Kca1.1 channel are also discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1M2S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http:// | + | 1M2S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha/beta scaffold]] | [[Category: alpha/beta scaffold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:59 2008'' |
Revision as of 11:51, 21 February 2008
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Solution Structure of A New Potassium Channels Blocker from the Venom of Chinese Scorpion Buthus martensi Karsch
Overview
This article reports the solution structure of BmTx3B (alpha-KTx16.2), a potassium channel blocker belonging to the subfamily alpha-KTx16, purified from the venom of the Chinese scorpion Buthus martensi Karsch. In solution, BmTx3B assumes a typical CSalphabeta motif, with an alpha-helix connected to a triple-stranded beta-sheet by 3 disulfide bridges, which belongs to the first structural group of short-chain scorpion toxins. On the other hand, BmTx3B is quite different from other toxins (such as ChTx and AgTx2) of this group in terms of the electrostatic and hydrophobic surface distribution. The functional surface (beta-face) of the molecule is characterized by less basic residues (only 2: Lys28 and Arg35) and extra aromatic residues (Phe1, Phe9, Trp15, and Tyr37). The peptide shows a great preference for the Kca1.1 channel over the Kv channel (about a 10(3)-fold difference). The model of BmTx3B/Kca1.1 channel complex generated by docking and dynamic simulation reveals that the stable binding between the BmTx3B and Kca1.1 channel is favored by a number of aromatic pi-pi stacking interactions. The influences of these structural features on the kinetic behavior of the toxin binding to Kca1.1 channel are also discussed.
About this Structure
1M2S is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.
Reference
The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx 16., Wang Y, Chen X, Zhang N, Wu G, Wu H, Proteins. 2005 Feb 1;58(2):489-97. PMID:15558557
Page seeded by OCA on Thu Feb 21 13:50:59 2008
Categories: Mesobuthus martensii | Single protein | Hu, G. | Li, M. | Wang, Y. | Wu, G. | Wu, H. | Zhang, N. | Alpha/beta scaffold
