7rz3 | pdb_00007rz3

The solution structure of remipede double-ICK toxin phi-Xibalbin3-Xt3a

spinqualitylabelsall models 7rz3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7rz3 is a 1 chain structure with sequence from Xibalbanus tulumensis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 10 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Multivalent ligands of ion channels have proven to be both very rare and highly valuable in yielding unique insights into channel structure and pharmacology. Here, we describe a bivalent peptide from the venom of Xibalbanus tulumensis, a troglobitic arthropod from the enigmatic class Remipedia, that causes persistent calcium release by activation of ion channels involved in muscle contraction. The high-resolution solution structure of phi-Xibalbin3-Xt3a reveals a tandem repeat arrangement of inhibitor-cysteine knot (ICK) domains previously only found in spider venoms. The individual repeats of Xt3a share sequence similarity with a family of scorpion toxins that target ryanodine receptors (RyR). Single-channel electrophysiology and quantification of released Ca(2+) stores within skinned muscle fibers confirm Xt3a as a bivalent RyR modulator. Our results reveal convergent evolution of RyR targeting toxins in remipede and scorpion venoms, while the tandem-ICK repeat architecture is an evolutionary innovation that is convergent with toxins from spider venoms. A bivalent remipede toxin promotes calcium release via ryanodine receptor activation.,Maxwell MJ, Thekkedam C, Lamboley C, Chin YK, Crawford T, Smith JJ, Liu J, Jia X, Vetter I, Laver DR, Launikonis BS, Dulhunty A, Undheim EAB, Mobli M Nat Commun. 2023 Feb 23;14(1):1036. doi: 10.1038/s41467-023-36579-w. PMID:36823422 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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