1h5o
From Proteopedia
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| - | [[Image:1h5o.gif|left|200px]] | + | [[Image:1h5o.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF CROTAMINE, A NEUROTOXIN FROM CROTALUS DURISSUS TERRIFICUS''' | + | {{Structure |
| + | |PDB= 1h5o |SIZE=350|CAPTION= <scene name='initialview01'>1h5o</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF CROTAMINE, A NEUROTOXIN FROM CROTALUS DURISSUS TERRIFICUS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H5O is a [ | + | 1H5O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5O OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom., Nicastro G, Franzoni L, de Chiara C, Mancin AC, Giglio JR, Spisni A, Eur J Biochem. 2003 May;270(9):1969-79. PMID:[http:// | + | Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom., Nicastro G, Franzoni L, de Chiara C, Mancin AC, Giglio JR, Spisni A, Eur J Biochem. 2003 May;270(9):1969-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12709056 12709056] |
[[Category: Crotalus durissus terrificus]] | [[Category: Crotalus durissus terrificus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:32:34 2008'' |
Revision as of 09:32, 20 March 2008
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SOLUTION STRUCTURE OF CROTAMINE, A NEUROTOXIN FROM CROTALUS DURISSUS TERRIFICUS
Overview
Crotamine is a component of the venom of the snake Crotalus durissus terrificus and it belongs to the myotoxin protein family. It is a 42 amino acid toxin cross-linked by three disulfide bridges and characterized by a mild toxicity (LD50 = 820 micro g per 25 g body weight, i.p. injection) when compared to other members of the same family. Nonetheless, it possesses a wide spectrum of biological functions. In fact, besides being able to specifically modify voltage-sensitive Na+ channel, it has been suggested to exhibit analgesic activity and to be myonecrotic. Here we report its solution structure determined by proton NMR spectroscopy. The secondary structure comprises a short N-terminal alpha-helix and a small antiparallel triple-stranded beta-sheet arranged in an alphabeta1beta2beta3 topology never found among toxins active on ion channels. Interestingly, some scorpion toxins characterized by a biological activity on Na+ channels similar to the one reported for crotamine, exhibit an alpha/beta fold, though with a beta1alphabeta2beta3 topology. In addition, as the antibacterial beta-defensins, crotamine interacts with lipid membranes. A comparison of crotamine with human beta-defensins shows a similar fold and a comparable net positive potential surface. To the best of our knowledge, this is the first report on the structure of a toxin from snake venom active on Na+ channel.
About this Structure
1H5O is a Single protein structure of sequence from Crotalus durissus terrificus. Full crystallographic information is available from OCA.
Reference
Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom., Nicastro G, Franzoni L, de Chiara C, Mancin AC, Giglio JR, Spisni A, Eur J Biochem. 2003 May;270(9):1969-79. PMID:12709056
Page seeded by OCA on Thu Mar 20 11:32:34 2008
