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Structure of the saxiphilin: saxitoxin (STX) complex reveals a convergent molecular recognition strategy for paralytic toxins

Sci Adv. 2019-06; 
Yen TJ, Lolicato M, Thomas-Tran R, Du Bois J, Minor DL Jr
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Bacterial Expression System The gene for North American bullfrog, R. catesbeiana, Sxph (GenBank: U05246.1), including its N-terminal secretory sequence, was codon-optimized and synthesized by GenScript. Get A Quote

摘要

Dinoflagelates and cyanobacteria produce saxitoxin (STX), a lethal bis-guanidinium neurotoxin causing paralytic shellfish poisoning. A number of metazoans have soluble STX-binding proteins that may prevent STX intoxication. However, their STX molecular recognition mechanisms remain unknown. Here, we present structures of saxiphilin (Sxph), a bullfrog high-affinity STX-binding protein, alone and bound to STX. The structures reveal a novel high-affinity STX-binding site built from a "proto-pocket" on a transferrin scaffold that also bears thyroglobulin domain protease inhibitor repeats. Comparison of Sxph and voltage-gated sodium channel STX-binding sites reveals a convergent toxin recognition strategy comprising... More

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