Bioinformatic analysis for structure and function of TCTP from Spirometra mansoni
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Parasitology
/
Phylogeny
/
Spirometra
/
Base Sequence
/
Biomarkers, Tumor
/
Helminth Proteins
/
Cestode Infections
/
Chemistry
/
Open Reading Frames
/
Amino Acid Sequence
Limits:
Animals
Language:
English
Journal:
Asian Pacific Journal of Tropical Medicine
Year:
2013
Type:
Article
Similar
MEDLINE
...
LILACS
LIS