2h9x | pdb_00002h9x

NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea

spinqualitylabelsall models 2h9x, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h9x is a 1 chain structure with sequence from Condylactis gigantea. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: HYP Resources: FirstGlance, OCA, RCSB, PDBsum 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 CgNa (Condylactis gigantea neurotoxin) is a 47-amino-acid- residue toxin from the giant Caribbean sea anemone Condylactis gigantea. The structure of CgNa, which was solved by 1H-NMR spectroscopy, is somewhat atypical and displays significant homology with both type I and II anemone toxins. CgNa also displays a considerable number of exceptions to the canonical structural elements that are thought to be essential for the activity of this group of toxins. Furthermore, unique residues in CgNa define a characteristic structure with strong negatively charged surface patches. These patches disrupt a surface-exposed cluster of hydrophobic residues present in all anemone-derived toxins described to date. A thorough characterization by patch-clamp analysis using rat DRG (dorsal root ganglion) neurons indicated that CgNa preferentially binds to TTX-S (tetrodotoxin-sensitive) voltage-gated sodium channels in the resting state. This association increased the inactivation time constant and the rate of recovery from inactivation, inducing a significant shift in the steady state of inactivation curve to the left. The specific structural features of CgNa may explain its weaker inhibitory capacity when compared with the other type I and II anemone toxins. CgNa, a type I toxin from the giant Caribbean sea anemone Condylactis gigantea shows structural similarities to both type I and II toxins, as well as distinctive structural and functional properties(1).,Salceda E, Perez-Castells J, Lopez-Mendez B, Garateix A, Salazar H, Lopez O, Aneiros A, Standker L, Beress L, Forssmann WG, Soto E, Jimenez-Barbero J, Gimenez-Gallego G Biochem J. 2007 Aug 15;406(1):67-76. PMID:17506725 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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