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Unique Mechanism of the Interaction between Honey Bee Toxin TPN[SUB]Q[/SUB] and rKir1.1 Potassium Channel Explored by Computational Simulations: Insights into the Relative Insensitivity of Channel towards Animal Toxins
The 21-residue compact tertiapin-Q (TPN[SUB]Q[/SUB]) toxin, a derivative of honey bee toxin tertiapin (TPN), is a potent blocker of inward-rectifier K[SUP]+[/SUP] channel subtype, rat Kir1.1 (rKir1.1) channel, and their interaction mechanism remains unclear. The interaction between honey bee toxin TPN[SUB]Q[/SUB] and rKir1.1 channel was systematically investigated by the computational approaches. The diverse and ubiquitous potassium channels serve a variety of physiological and pharmacological functions [1]. These proteins are often targeted by numerous peptide toxins from the venomous animals, such as scorpions, spiders, sea anemones, honey bees, snakes and cone snails [2]. With more potassium channels as the therapeutic targets [8], the rational screening and design of peptide drugs, based on the structural information on the potassium channel-animal toxin interactions, exhibited an attractive prospect for disease diagnosis and treatment [9]–[12].
http://www.plosone.org/article/info:doi/10.1371/journal.pone.0067213
 
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