View source for 1h5o

==Solution structure of Crotamine, a neurotoxin from Crotalus durissus terrificus==
<StructureSection load='1h5o' size='340' side='right' caption='[[1h5o]], [[NMR_Ensembles_of_Models | 26 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1h5o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crotalus_durissus_terrificus Crotalus durissus terrificus]. 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><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>
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== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h5o_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:12709056</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Crotamine|Crotamine]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Crotalus durissus terrificus]]
[[Category: Chiara, C De.]]
[[Category: Franzoni, L.]]
[[Category: Giglio, J R.]]
[[Category: Mancin, C A.]]
[[Category: Nicastro, G.]]
[[Category: Spisni, A.]]
[[Category: Sodium channel affecting toxin]]
[[Category: Toxin]]
[[Category: Venom]]