1b7d
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(New page: 200px<br /><applet load="1b7d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b7d, resolution 1.73Å" /> '''NEUROTOXIN (TS1) FRO...)
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Revision as of 09:18, 20 November 2007
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NEUROTOXIN (TS1) FROM BRAZILIAN SCORPION TITYUS SERRULATUS
Overview
The crystal structure of neurotoxin Ts1, a major component of the venom of, the Brazilian scorpion Tityus serrulatus, has been determined at 1.7 A, 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.
About this Structure
1B7D is a Single protein structure of sequence from Tityus serrulatus with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins., Polikarpov I, Junior MS, Marangoni S, Toyama MH, Teplyakov A, J Mol Biol. 1999 Jul 2;290(1):175-84. PMID:10388565
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