2bmt

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmt OCA], [http://www.ebi.ac.uk/pdbsum/2bmt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bmt RCSB]</span>
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'''SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES'''
'''SCORPION TOXIN BMTX2 FROM BUTHUS MARTENSII KARSCH, NMR, 25 STRUCTURES'''
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[[Category: Nakajima, T.]]
[[Category: Nakajima, T.]]
[[Category: Romi-Lebrun, R.]]
[[Category: Romi-Lebrun, R.]]
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[[Category: buthus martensii]]
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[[Category: Buthus martensii]]
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[[Category: large conductance potassium channel]]
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[[Category: Large conductance potassium channel]]
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[[Category: neurotoxin]]
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[[Category: Neurotoxin]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: scorpion]]
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[[Category: Scorpion]]
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[[Category: structure]]
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[[Category: Structure]]
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[[Category: voltage gated potassium channel]]
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[[Category: Voltage gated potassium channel]]
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Revision as of 17:30, 3 May 2008

Template:STRUCTURE 2bmt

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 Page seeded by OCA on Sat May 3 20:30:32 2008

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