1txm
From Proteopedia
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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 NH2 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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