Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins

dc.creatorPolikarpov, I
dc.creatorMatilde, MS
dc.creatorMarangoni, S
dc.creatorToyama, MH
dc.creatorTeplyakov, A
dc.date1999
dc.date37438
dc.date2014-12-02T16:28:32Z
dc.date2015-11-26T16:37:06Z
dc.date2014-12-02T16:28:32Z
dc.date2015-11-26T16:37:06Z
dc.date.accessioned2018-03-28T23:20:06Z
dc.date.available2018-03-28T23:20:06Z
dc.identifierJournal Of Molecular Biology. Academic Press Ltd, v. 290, n. 1, n. 175, n. 184, 1999.
dc.identifier0022-2836
dc.identifierWOS:000081311300013
dc.identifier10.1006/jmbi.1999.2868
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/57448
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/57448
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/57448
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1271965
dc.descriptionThe crystal structure of neurotoxin Ts1, a major component of the venom of the Brazilian scorpion Tityus serrulatus, has been determined at 1.7 Angstrom resolution. It is the first X-ray structure of a highly toxic anti-mammalian beta-toxin. The folding of the polypeptide chain of Ts1 is similar to that of other scorpion toxins. A cysteine-stabilised alpha-helix/beta-sheet motif forms the core of the flattened molecule All residues identified as functionally important by Chemical modification and site-directed mutagenesis are located on one side of the molecule, which is therefore considered as the Na+ channel recognition site. The distribution of charged and non-polar residues over this surface determines the specificity of the toxin-channel interaction. Comparison to other scorpion toxins shows that positively charged groups at positions 1 and 12 as well as a negative charge at position 2 are likely determinants of the specificity of beta-toxins. In contrast, the contribution of the conserved aromatic cluster to the interaction might be relatively small. Comparison of Ts1 to weak beta-toxins from Centruroides sculpturatus Ewing reveals that a number of basic amino acid residues located on the face of the molecule opposite to the binding surface may account for the high toxicity of Ts1. (C) 1999 Academic Press.
dc.description290
dc.description1
dc.description175
dc.description184
dc.languageen
dc.publisherAcademic Press Ltd
dc.publisherLondon
dc.publisherInglaterra
dc.relationJournal Of Molecular Biology
dc.relationJ. Mol. Biol.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectscorpion neurotoxin
dc.subjectTityus serrulatus
dc.subjectcrystal structure
dc.subjectsodium channel
dc.subjectAndroctonus-australis-hector
dc.subjectNuclear-magnetic-resonance
dc.subjectInsect-specific Toxin
dc.subjectAmino-acid-sequence
dc.subjectSodium-channel
dc.subject3-dimensional Structure
dc.subjectAngstrom Resolution
dc.subjectCentruroides-noxius
dc.subjectAntiinsect Toxin
dc.subjectReceptor-sites
dc.titleCrystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins
dc.typeArtículos de revistas


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