1tsk

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tsk OCA], [http://www.ebi.ac.uk/pdbsum/1tsk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tsk RCSB]</span>
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'''SCORPION TOXIN (TS KAPPA) FROM TITYUS SERRULATUS ACTIVE ON SMALL CONDUCTANCE POTASSIUM CHANNEL, NMR, 30 STRUCTURES'''
'''SCORPION TOXIN (TS KAPPA) FROM TITYUS SERRULATUS ACTIVE ON SMALL CONDUCTANCE POTASSIUM CHANNEL, NMR, 30 STRUCTURES'''
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[[Category: Blanc, E.]]
[[Category: Blanc, E.]]
[[Category: Darbon, H.]]
[[Category: Darbon, H.]]
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[[Category: neurotoxin]]
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[[Category: Neurotoxin]]
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[[Category: potassium channel]]
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[[Category: Potassium channel]]
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[[Category: scorpion]]
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[[Category: Scorpion]]
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[[Category: tityus serrulatus]]
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[[Category: Tityus serrulatus]]
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[[Category: toxin]]
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[[Category: Toxin]]
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[[Category: ts kapa]]
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[[Category: Ts kapa]]
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Revision as of 07:18, 3 May 2008

Template:STRUCTURE 1tsk

SCORPION TOXIN (TS KAPPA) FROM TITYUS SERRULATUS ACTIVE ON SMALL CONDUCTANCE POTASSIUM CHANNEL, NMR, 30 STRUCTURES


Overview

TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small-conductance apamin-sensitive calcium-activated potassium channels (SK). It is able to efficiently compete with apamin for binding on this channel (K0.5 = 0.3 nM) [Legros, C. et al., FEBS Lett. 390:81-84, 1996]. The solution structure of TsK has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a short alpha helix from residues 14 to 20 and a three-stranded antiparallel beta sheet (residues 2-3, 27-29, and 32-34). The interaction of TsK with the SK potassium channel has been modeled according to the charge anisotropy of the ligand. The resulting dipole moment orientates TsK so that it presents toward the receptor, a surface, mainly basic, encompassing residues K18 and K19 on one side and R9 and Y8 on the other. Despite its three-dimensional structure that is related with scorpion toxins active on voltage-gated potassium channels such as charybdotoxin, the pharmacological activity and specificity of TsK is related with shorter scorpion toxins (i.e., possessing an only two-stranded beta sheet) such as scyllatoxin (also named leiurotoxin I) or P05.

About this Structure

1TSK is a Single protein structure of sequence from Tityus serrulatus. Full crystallographic information is available from OCA.

Reference

Solution structure of TsKapa, a charybdotoxin-like scorpion toxin from Tityus serrulatus with high affinity for apamin-sensitive Ca(2+)-activated K+ channels., Blanc E, Lecomte C, Rietschoten JV, Sabatier JM, Darbon H, Proteins. 1997 Nov;29(3):359-69. PMID:9365990 Page seeded by OCA on Sat May 3 10:18:58 2008

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