8v66

Nanorana parkeri saxiphilin:GTX5 (co-crystal)

spinqualitylabelsall models 8v66, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8v66 is a 1 chain structure with sequence from Nanorana parkeri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: 1PE, YGZ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A9X9ZA84_9NEOB Publication Abstract from PubMed Dinoflagellates and cyanobacteria produce saxitoxin (STX) and ~50 congeners that disrupt bioelectrical signals by blocking voltage-gated sodium channels (Na(V)s). Consuming seafood carrying these toxins causes paralytic shellfish poisoning (PSP). Although Na(V)s and anuran STX binding proteins (saxiphilins, Sxphs) use convergent STX binding modes, the structural basis for STX congener recognition is unknown. Here, we show that American bullfrog (Rana catesbeiana) RcSxph and High Himalaya frog (Nanorana parkeri) NpSxph sequester STX congeners using a 'lock and key' mode shared with STX. Importantly, functional studies demonstrate that Sxph 'toxin sponges' reverse Na(V) block by multiple STX congeners and detect these toxins in a radioligand binding assay (RBA) used for environmental testing. Together, our study establishes how Sxphs sequester select neurotoxins and uncover STX congener-specific interactions distinct from Na(V)s. These findings expand understanding of toxin sponge action and provide a foundation for strategies to monitor and mitigate the harmful effects of STX congeners. Structural basis for saxitoxin congener binding and neutralization by anuran saxiphilins.,Zakrzewska S, Nixon SA, Chen Z, Hajare HS, Park ER, Mulcahy JV, Arlinghaus KM, Neu E, Konovalov K, Provasi D, Leighfield TA, Filizola M, Du Bois J, Minor DL Jr Nat Commun. 2025 Apr 24;16(1):3885. doi: 10.1038/s41467-025-58903-2. PMID:40274765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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