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Asian Pacific Journal of Tropical Medicine ; (12): 709-712, 2013.
Article in English | WPRIM | ID: wpr-819978

ABSTRACT

OBJECTIVE@#To predict structure and function of translationally controlled tumor protein (TCTP) from Spirometra mansoni by bioinformatics technology, and to provide a theoretical basis for further study.@*METHODS@#Open reading frame (ORF) of EST sequence from Spirometra mansoni was obtained by ORF finder and was translated into amino acid residue by DNAclub. The structure domain was analyzed by Blast. By the method of online analysis tools: Protparam, InterProScan, protscale, SignalP-3.0, PSORT II, BepiPred, TMHMM, VectorNTI Suite 9 packages and Phyre2, the structure and function of the protein were predicted and analyzed.@*RESULTS@#The results showed that the EST sequence was Sm TCTP with 173 amino acid residues, theoretical molecular weight was 19 872.0 Da. The protein has the closest evolutionary status with Clonorchis sinensis, Schistosoma mansoni, and Schistosoma japonicum. Then it had no signal peptide site and transmembrane domain. Secondary structure of TCTP contained two α -helices and eight β -strands.@*CONCLUSIONS@#Sm TCTP was a variety of biological functions of protein that may be used as a vaccine candidate molecule and drug target.


Subject(s)
Animals , Dogs , Amino Acid Sequence , Base Sequence , Biomarkers, Tumor , Chemistry , Genetics , Metabolism , Cestode Infections , Parasitology , Computational Biology , Dog Diseases , Expressed Sequence Tags , Helminth Proteins , Chemistry , Genetics , Metabolism , Helminths , Chemistry , Classification , Genetics , Open Reading Frames , Phylogeny , Protein Structure, Secondary , Protein Structure, Tertiary , Spirometra , Chemistry , Genetics , Metabolism , Parasitology
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