1txm
From Proteopedia
(New page: 200px<br /><applet load="1txm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1txm" /> '''SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAU...) |
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| - | [[Image:1txm.gif|left|200px]]<br /><applet load="1txm" size=" | + | [[Image:1txm.gif|left|200px]]<br /><applet load="1txm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1txm" /> | caption="1txm" /> | ||
'''SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES'''<br /> | '''SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent | + | Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd = 37 nM), Kv1.2 (Kd = 0.8 nM), Kv1.3 (Kd = 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activated potassium channels. It has a unique disulfide pairing among the scorpion toxins family. The solution structure of MTX has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a bended helix from residues 6 to 16 connected by a loop to a two-stranded antiparallel beta sheet (residues 23 to 26 and 28 to 31). The interaction of MTX with the pore region of the Kv1.2 potassium channel has been modeled according to their charge anisotropy. The structure of MTX is similar to other short scorpion toxins despite its peculiar disulfide pairing. Its interaction with the Kv1.2 channel involves a dipole moment, which guides and orients the toxin onto the pore, toward the binding site, and which thus is responsible for the specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1TXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scorpio_maurus Scorpio maurus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scorpio_maurus Scorpio maurus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Scorpio maurus]] | [[Category: Scorpio maurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ayeb, M | + | [[Category: Ayeb, M El.]] |
[[Category: Blanc, E.]] | [[Category: Blanc, E.]] | ||
[[Category: Darbon, H.]] | [[Category: Darbon, H.]] | ||
[[Category: Kharrat, R.]] | [[Category: Kharrat, R.]] | ||
[[Category: Meunier, S.]] | [[Category: Meunier, S.]] | ||
| - | [[Category: Rietschoten, J | + | [[Category: Rietschoten, J Van.]] |
| - | [[Category: Sabatier, J | + | [[Category: Sabatier, J M.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: alpha beta scorpion toxin fold]] | [[Category: alpha beta scorpion toxin fold]] | ||
| Line 27: | Line 27: | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:24 2008'' |
Revision as of 13:18, 21 February 2008
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SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES
Overview
Maurotoxin (MTX), purified from the scorpionid Scorpio maurus is a potent ligand for potassium channels. It shows a broad specificity as being active on Kv1.1 (Kd = 37 nM), Kv1.2 (Kd = 0.8 nM), Kv1.3 (Kd = 150 nM) voltage-gated potassium channels, as well as on small-conductance calcium-activated potassium channels. It has a unique disulfide pairing among the scorpion toxins family. The solution structure of MTX has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a bended helix from residues 6 to 16 connected by a loop to a two-stranded antiparallel beta sheet (residues 23 to 26 and 28 to 31). The interaction of MTX with the pore region of the Kv1.2 potassium channel has been modeled according to their charge anisotropy. The structure of MTX is similar to other short scorpion toxins despite its peculiar disulfide pairing. Its interaction with the Kv1.2 channel involves a dipole moment, which guides and orients the toxin onto the pore, toward the binding site, and which thus is responsible for the specificity.
About this Structure
1TXM is a Single protein structure of sequence from Scorpio maurus with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels., Blanc E, Sabatier JM, Kharrat R, Meunier S, el Ayeb M, Van Rietschoten J, Darbon H, Proteins. 1997 Nov;29(3):321-33. PMID:9365987
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