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1bmr

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{{STRUCTURE_1bmr| PDB=1bmr | SCENE= }}
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'''ALPHA-LIKE TOXIN LQH III FROM SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS, NMR, 25 STRUCTURES'''
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===ALPHA-LIKE TOXIN LQH III FROM SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS, NMR, 25 STRUCTURES===
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==Overview==
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NMR structures of a new toxin from the scorpion Leiurus quinquestriatus hebraeus (Lqh III) have been investigated in conjunction with its pharmacological properties. This toxin is proposed to belong to a new group of scorpion toxins, the alpha-like toxins that target voltage-gated sodium channels with specific properties compared with the classical alpha-scorpion toxins. Electrophysiological analysis showed that Lqh III inhibits a sodium current inactivation in the cockroach axon, but induces in addition a resting depolarization due to a slowly decaying tail current atypical to other alpha-toxin action. Binding studies indicated that radiolabeled Lqh III binds with a high degree of affinity (Ki=2.2 nM) on cockroach sodium channels and that the alpha-toxin from L quinquestriatus hebraeus highly active on insects (LqhalphaIT) and alpha-like toxins compete at low concentration for its receptor binding site, suggesting that the alpha-like toxin receptor site is partially overlapping with the receptor site 3. Conversely, in rat brain, Lqh III competes for binding of the most potent anti-mammal alpha-toxin from Androctonus australis Hector venom (AaH II) only at very high concentration.The NMR structures were used for the scrutiny of the similarities and differences with representative scorpion alpha-toxins targeting the voltage-gated sodium channels of either mammals or insects. Three turn regions involved in the functional binding site of the anti-insect LqhalphaIT toxin reveal significant differences in the Lqh III structure. The electrostatic charge distribution in the Lqh III toxin is also surprisingly different when compared with the anti-mammal alpha-toxin AaH II. Similarities in the electrostatic charge distribution are, however, recognized between alpha-toxins highly active on insects and the alpha-like toxin Lqh III. This affords additional important elements to the definition of the new alpha-like group of scorpion toxins and the mammal versus insect scorpion toxin selectivities.
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{{ABSTRACT_PUBMED_9917409}}
==About this Structure==
==About this Structure==
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1BMR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leiurus_quinquestriatus_hebraeus Leiurus quinquestriatus hebraeus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMR OCA].
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1BMR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leiurus_quinquestriatus_hebraeus Leiurus quinquestriatus hebraeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMR OCA].
==Reference==
==Reference==
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[[Category: Scorpion toxin]]
[[Category: Scorpion toxin]]
[[Category: Sodium channel inhibitor]]
[[Category: Sodium channel inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:42:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:23:39 2008''

Revision as of 16:23, 30 June 2008

Image:1bmr.png

Template:STRUCTURE 1bmr

ALPHA-LIKE TOXIN LQH III FROM SCORPION LEIURUS QUINQUESTRIATUS HEBRAEUS, NMR, 25 STRUCTURES

Template:ABSTRACT PUBMED 9917409

About this Structure

1BMR is a Single protein structure of sequence from Leiurus quinquestriatus hebraeus. Full experimental information is available from OCA.

Reference

NMR structures and activity of a novel alpha-like toxin from the scorpion Leiurus quinquestriatus hebraeus., Krimm I, Gilles N, Sautiere P, Stankiewicz M, Pelhate M, Gordon D, Lancelin JM, J Mol Biol. 1999 Jan 29;285(4):1749-63. PMID:9917409

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