2h9x
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2h9x.jpg|left|200px]] | [[Image:2h9x.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2h9x", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2h9x| PDB=2h9x | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea''' | '''NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea''' | ||
| Line 29: | Line 26: | ||
[[Category: Lopez-Mendez, B.]] | [[Category: Lopez-Mendez, B.]] | ||
[[Category: Perez-Castells, J.]] | [[Category: Perez-Castells, J.]] | ||
| - | [[Category: | + | [[Category: Beta sheet]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:02:15 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:02, 4 May 2008
NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea
Overview
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.
About this Structure
2H9X is a Single protein structure of sequence from Condylactis gigantea. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 06:02:15 2008
