Structural highlights
Function[3S1CC_NAJAT] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Has a lower toxicity than cobrotoxin.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBy using single wavelength anomalous diffraction phasing based on the anomalous signal from copper atoms, the crystal structure of atratoxin was determined at the resolution of 1.5 A and was refined to an ultrahigh resolution of 0.87 A. The ultrahigh resolution electron density maps allowed the modeling of 38 amino acid residues in alternate conformations and the location of 322 of 870 possible hydrogen atoms. To get accurate information at the atomic level, atratoxin-b (an analog of atratoxin with reduced toxicity) was also refined to an atomic resolution of 0.92 A. By the sequence and structural comparison of these two atratoxins, Arg(33) and Arg(36) were identified to be critical to their varied toxicity. The effect of copper ions on the distribution of hydrogen atoms in atratoxin was discussed, and the interactions between copper ions and protein residues were analyzed based on a statistical method, revealing a novel pentahedral copper-binding motif. The atomic resolution crystal structure of atratoxin determined by single wavelength anomalous diffraction phasing.,Lou X, Liu Q, Tu X, Wang J, Teng M, Niu L, Schuller DJ, Huang Q, Hao Q J Biol Chem. 2004 Sep 10;279(37):39094-104. Epub 2004 Jul 12. PMID:15252034[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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