1h5o: Difference between revisions
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<StructureSection load='1h5o' size='340' side='right' caption='[[1h5o]], [[NMR_Ensembles_of_Models | 26 NMR models]]' scene=''> | <StructureSection load='1h5o' size='340' side='right' caption='[[1h5o]], [[NMR_Ensembles_of_Models | 26 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h5o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1h5o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crodu Crodu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5O FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1h5o RCSB], [http://www.ebi.ac.uk/pdbsum/1h5o PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1h5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h5o RCSB], [http://www.ebi.ac.uk/pdbsum/1h5o PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1h5o" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Crodu]] | ||
[[Category: Chiara, C De]] | [[Category: Chiara, C De]] | ||
[[Category: Franzoni, L]] | [[Category: Franzoni, L]] | ||
Revision as of 05:47, 11 September 2015
Solution structure of Crotamine, a neurotoxin from Crotalus durissus terrificusSolution structure of Crotamine, a neurotoxin from Crotalus durissus terrificus
Structural highlights
Function[MYXC_CRODU] This toxin specifically modifies voltage-gated sodium channels (Nav), it exhibits analgesic activity and causes severe muscle necrosis by a non-enzymatic mechanism. Moreover, it actively interacts with lipid membranes.[1] [2] 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 PubMedCrotamine 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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