2kja | pdb_00002kja

Chemical shift assignments, constraints, and coordinates for CN5 scorpion toxin

spinqualitylabelsall models 2kja, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kja is a 1 chain structure with sequence from Centruroides noxius. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [SCX5_CENNO] Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is lethal to crustaceans (freshwater crayfish (Cambarellus montezumae spp.)), it provokes a reversible paralysis to insects (crickets (Achaeta spp.)), but is not toxic to mice. At high concentrations, it does displace the (beta) mammal-specific toxin Cn2 from rat brain synaptosomes. 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 PubMed The crustacean toxin Cn5 from Centruroides noxius Hoffmann and peptide Css39.8 from Centruroides suffusus suffusus scorpion venoms are identical peptides, as confirmed by amino acid sequence of purified toxins and by DNA sequencing of the two respective cloned genes. Therefore in this communication they will be simply named Cn5. Cn5 is a 66 amino acid long peptide with four disulfide bridges, formed between pairs of cysteines: C1-C8, C2-C5, C3-C6, and C4-C7 (the numbers indicate the relative positions of the cysteine residues in the primary structure). This peptide is non-toxic to mammals but deadly to arthropods (LD(50) 28.5 mg/g body weight of crayfish). Its three-dimensional structure was determined by NMR using a total of 965 meaningful distance constraints derived from the volume integration of the 2D NOESY spectra. The Cn5 structure displays a mixed alpha/beta fold stabilized by four disulfide bridges, with a kink induced by a cis-proline in its C-terminal part. Cn5 electrostatic surface is compared to that of Cn2 toxin toxic to mammals. The local differences produced by additional or substituted residues that would influence toxin selectivity towards mammalian or crustacean Na(+) channels are discussed. Solution structure of Cn5, a crustacean toxin found in the venom of the scorpions Centruroides noxius and Centruroides suffusus suffusus.,Corzo G, Prochnicka-Chalufour A, Garcia BI, Possani LD, Delepierre M Biochim Biophys Acta. 2009 Nov;1794(11):1591-8. Epub 2009 Jul 21. PMID:19631296 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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