2h9x
From Proteopedia
(New page: 200px<br /><applet load="2h9x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h9x" /> '''NMR structure for the CgNa toxin from the se...) |
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'''NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea'''<br /> | '''NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2H9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Condylactis_gigantea Condylactis gigantea]. Full crystallographic information is available from [http:// | + | 2H9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Condylactis_gigantea Condylactis gigantea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H9X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta sheet]] | [[Category: beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:00:19 2008'' |
Revision as of 13:00, 23 January 2008
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NMR structure for the CgNa toxin from the sea anemone Condylactis gigantea
Overview
CgNa is a toxin from the sea anemone Condylactis gigantea that is, comprised of 47-residues. The structure of CgNa, solved by 1H NMR, spectroscopy, is somewhat atypical, displaying significant homologies to, both type I and II anemonae toxins, as well as a considerable number of, exceptions to what are considered as canonical structural elements of this, group of toxins, and that are thought to be essential for their activity., 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 the toxins, described in this group to date. A thorough characterization by, patch-clamp using rat dorsal root ganglion neurons indicate that CgNa, preferentially binds to TTX-S Na + channels in the resting state. This, association increases the inactivation time constant and the rate of, recovery from inactivation, inducing a significant shift to the left in, the steady state of the inactivation curve. The specific structural, features of CgNa may explain its weaker inhibitory capacity when compared, to 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 sea anemone Condylactis gigantea shows structural similarities to both type I and II toxins, as well as distinctive structural and functional properties., 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 May 16;. PMID:17506725
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