Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels

dc.creatorPinheiro, CB
dc.creatorMarangoni, S
dc.creatorToyama, MH
dc.creatorPolikarpov, I
dc.date2003
dc.dateMAR
dc.date2014-08-01T18:29:24Z
dc.date2015-11-26T18:04:37Z
dc.date2014-08-01T18:29:24Z
dc.date2015-11-26T18:04:37Z
dc.date.accessioned2018-03-29T00:46:46Z
dc.date.available2018-03-29T00:46:46Z
dc.identifierActa Crystallographica Section D-biological Crystallography. Blackwell Munksgaard, v. 59, n. 405, n. 415, 2003.
dc.identifier0907-4449
dc.identifierWOS:000181609800001
dc.identifier10.1107/S090744490202111X
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/79628
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/79628
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1292904
dc.descriptionThe structure of the Ts1 toxin from the Brazilian scorpion Tityus serrulatus was investigated at atomic resolution using X-ray crystallography. Several positively charged niches exist on the Ts1 molecular surface, two of which were found to coordinate phosphate ions present in the crystallization solution. One phosphate ion is bound to the conserved basic Lys1 residue at the Ts1 N-terminus and to residue Asn49. The second ion was found to be caged by residues Lys12, Trp54 and Arg56. Lys12 and Tyr/Trp54 residues are strictly conserved in all classical scorpion beta-neurotoxins. The cavity formed by these residues may represent a special scaffold required for interaction between beta-neurotoxins and sodium channels. The charge distribution on the Ts1 surface and the results of earlier chemical modification studies and side-directed mutagenesis experiments strongly indicate that the phosphate-ion positions mark plausible binding sites to the Na+ channel. The existence of two distinct binding sites on the Ts1 molecular surface provides an explanation for the competition between Ts1, depressant (LqhIT2) and excitatory (AaHIT) neurotoxins.
dc.description59
dc.description3
dc.description405
dc.description415
dc.languageen
dc.publisherBlackwell Munksgaard
dc.publisherCopenhagen
dc.publisherDinamarca
dc.relationActa Crystallographica Section D-biological Crystallography
dc.relationActa Crystallogr. Sect. D-Biol. Crystallogr.
dc.rightsaberto
dc.sourceWeb of Science
dc.subjectScorpion Centruroides-sculpturatus
dc.subjectProtein Crystallography Beamline
dc.subjectDepressant Insect Toxin
dc.subjectButhus-martensii Karsch
dc.subjectSodium-channels
dc.subjectReceptor-sites
dc.subjectCrystal-structure
dc.subjectHigh-affinity
dc.subjectRat-brain
dc.subjectAngstrom Resolution
dc.titleStructural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels
dc.typeArtículos de revistas


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