dc.creator | Polikarpov, I | |
dc.creator | Matilde, MS | |
dc.creator | Marangoni, S | |
dc.creator | Toyama, MH | |
dc.creator | Teplyakov, A | |
dc.date | 1999 | |
dc.date | 37438 | |
dc.date | 2014-12-02T16:28:32Z | |
dc.date | 2015-11-26T16:37:06Z | |
dc.date | 2014-12-02T16:28:32Z | |
dc.date | 2015-11-26T16:37:06Z | |
dc.date.accessioned | 2018-03-28T23:20:06Z | |
dc.date.available | 2018-03-28T23:20:06Z | |
dc.identifier | Journal Of Molecular Biology. Academic Press Ltd, v. 290, n. 1, n. 175, n. 184, 1999. | |
dc.identifier | 0022-2836 | |
dc.identifier | WOS:000081311300013 | |
dc.identifier | 10.1006/jmbi.1999.2868 | |
dc.identifier | http://www.repositorio.unicamp.br/jspui/handle/REPOSIP/57448 | |
dc.identifier | http://www.repositorio.unicamp.br/handle/REPOSIP/57448 | |
dc.identifier | http://repositorio.unicamp.br/jspui/handle/REPOSIP/57448 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1271965 | |
dc.description | The 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.description | 290 | |
dc.description | 1 | |
dc.description | 175 | |
dc.description | 184 | |
dc.language | en | |
dc.publisher | Academic Press Ltd | |
dc.publisher | London | |
dc.publisher | Inglaterra | |
dc.relation | Journal Of Molecular Biology | |
dc.relation | J. Mol. Biol. | |
dc.rights | fechado | |
dc.source | Web of Science | |
dc.subject | scorpion neurotoxin | |
dc.subject | Tityus serrulatus | |
dc.subject | crystal structure | |
dc.subject | sodium channel | |
dc.subject | Androctonus-australis-hector | |
dc.subject | Nuclear-magnetic-resonance | |
dc.subject | Insect-specific Toxin | |
dc.subject | Amino-acid-sequence | |
dc.subject | Sodium-channel | |
dc.subject | 3-dimensional Structure | |
dc.subject | Angstrom Resolution | |
dc.subject | Centruroides-noxius | |
dc.subject | Antiinsect Toxin | |
dc.subject | Receptor-sites | |
dc.title | Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins | |
dc.type | Artículos de revistas | |