کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10880361 | 1076960 | 2007 | 21 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The differential preference of scorpion α-toxins for insect or mammalian sodium channels: Implications for improved insect control
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The differential preference of scorpion α-toxins for insect or mammalian sodium channels: Implications for improved insect control The differential preference of scorpion α-toxins for insect or mammalian sodium channels: Implications for improved insect control](/preview/png/10880361.png)
چکیده انگلیسی
Receptor site-3 on voltage-gated sodium channels is targeted by a variety of structurally distinct toxins from scorpions, sea anemones, and spiders whose typical action is the inhibition of sodium current inactivation. This site interacts allosterically with other topologically distinct receptors that bind alkaloids, lypophilic polyether toxins, pyrethroids, and site-4 scorpion toxins. These features suggest that design of insecticides with specificity for site-3 might be rewarding due to the positive cooperativity with other toxins or insecticidal agents. Yet, despite the central role of scorpion α-toxins in envenomation and their vast use in the study of channel functions, molecular details on site-3 are scarce. Scorpion α-toxins vary greatly in preference for sodium channels of insects and mammals, and some of them are highly active on insects. This implies that despite its commonality, receptor site-3 varies on insect vs. mammalian channels, and that elucidation of these differences could potentially be exploited for manipulation of toxin preference. This review provides current perspectives on (i) the classification of scorpion α-toxins, (ii) their mode of interaction with sodium channels and pharmacological divergence, (iii) molecular details on their bioactive surfaces and differences associated with preference for channel subtypes, as well as (iv) a summary of the present knowledge about elements involved in constituting receptor site-3. These details, combined with the variations in allosteric interactions between site-3 and the other receptor sites on insect and mammalian sodium channels, may be useful in new strategies of insect control and future design of anti-insect selective ligands.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 49, Issue 4, 15 March 2007, Pages 452-472
Journal: Toxicon - Volume 49, Issue 4, 15 March 2007, Pages 452-472
نویسندگان
Dalia Gordon, Izhar Karbat, Nitza Ilan, Lior Cohen, Roy Kahn, Nicolas Gilles, Ke Dong, Walter Stühmer, Jan Tytgat, Michael Gurevitz,