1h5o

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5o OCA], [http://www.ebi.ac.uk/pdbsum/1h5o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h5o RCSB]</span>
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'''SOLUTION STRUCTURE OF CROTAMINE, A NEUROTOXIN FROM CROTALUS DURISSUS TERRIFICUS'''
'''SOLUTION STRUCTURE OF CROTAMINE, A NEUROTOXIN FROM CROTALUS DURISSUS TERRIFICUS'''
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[[Category: Nicastro, G.]]
[[Category: Nicastro, G.]]
[[Category: Spisni, A.]]
[[Category: Spisni, A.]]
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[[Category: neurotoxin]]
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[[Category: Neurotoxin]]
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[[Category: sodium channel affecting toxin]]
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[[Category: Sodium channel affecting toxin]]
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[[Category: toxin]]
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[[Category: Toxin]]
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[[Category: venom]]
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[[Category: Venom]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:13 2008''
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Revision as of 15:27, 2 May 2008

Template:STRUCTURE 1h5o

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 Fri May 2 18:27:57 2008

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