2bmt
From Proteopedia
(New page: 200px<br /><applet load="2bmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bmt" /> '''SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII K...) |
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| - | [[Image:2bmt.jpg|left|200px]]<br /><applet load="2bmt" size=" | + | [[Image:2bmt.jpg|left|200px]]<br /><applet load="2bmt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bmt" /> | caption="2bmt" /> | ||
'''SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES'''<br /> | '''SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of BmTX2 purified from the venom of the Chinese | + | The solution structure of BmTX2 purified from the venom of the Chinese Buthid Buthus martensi has been determined by 2D NMR spectroscopy techniques which led to the description of its 3D conformation. The structure consists of a triple-stranded beta-sheet connected to a helical structure. This helix encompasses 10 residues, from 11 to 20, begins with a turn of 310 helix, and ends with an alpha helix. The three strands of beta sheet comprise residues 2-6, with a bulge covering residues 4 and 5, 26-29, and 32-35, with a type I' beta turn centered on residues 30-31. We also characterized the solution structure of BmTX1. The two toxins which are potent blockers of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1. 3) are highly superimposable and possess the same structural characteristics. Analysis of these structures allows us to hypothesize that, besides the main surface of interaction described by the functional map of charybdotoxin, one can expect that the binding of scorpion toxins on BKCa channels may involve residues on the edge of this surface. |
==About this Structure== | ==About this Structure== | ||
| - | 2BMT 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:// | + | 2BMT 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=2BMT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: voltage gated potassium channel]] | [[Category: voltage gated potassium channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:24 2008'' |
Revision as of 14:39, 21 February 2008
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SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES
Overview
The solution structure of BmTX2 purified from the venom of the Chinese Buthid Buthus martensi has been determined by 2D NMR spectroscopy techniques which led to the description of its 3D conformation. The structure consists of a triple-stranded beta-sheet connected to a helical structure. This helix encompasses 10 residues, from 11 to 20, begins with a turn of 310 helix, and ends with an alpha helix. The three strands of beta sheet comprise residues 2-6, with a bulge covering residues 4 and 5, 26-29, and 32-35, with a type I' beta turn centered on residues 30-31. We also characterized the solution structure of BmTX1. The two toxins which are potent blockers of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1. 3) are highly superimposable and possess the same structural characteristics. Analysis of these structures allows us to hypothesize that, besides the main surface of interaction described by the functional map of charybdotoxin, one can expect that the binding of scorpion toxins on BKCa channels may involve residues on the edge of this surface.
About this Structure
2BMT is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.
Reference
Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels., Blanc E, Romi-Lebrun R, Bornet O, Nakajima T, Darbon H, Biochemistry. 1998 Sep 8;37(36):12412-8. PMID:9730813
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