Prediction and Analysis of Three-Dimensional Structure of the p7- Transactivated Protein1 of Hepatitis C Virus.

Autor:	El Hefnawi MM; Informatics and Systems Department, Division of Engineering Research Sciences, the National Research Centre, Giza, Egypt., Hasan ME; Bioinformatics Department, Genetic Engineering and Biotechnology Research Institute, Sadat City University, Sadat, Egypt., Mahmoud A; Bioinformatics Department, Genetic Engineering and Biotechnology Research Institute, Sadat City University, Sadat, Egypt.; Department of Biology, College of Science, Imam Abdulrahman Bin Faisal University, Damam, Saudi Arabia., Khidr YA; Plant Biotechnology Department, Genetic Engineering and Biotechnology Research Institute, Sadat City University, Sadat, Egypt., El Behaidy WH; Computer Science Department, Helwan University, Ain Helwan, Egypt., El-Absawy EA; Bioinformatics Department, Genetic Engineering and Biotechnology Research Institute, Sadat City University, Sadat, Egypt., Hemeida AA; Bioinformatics Department, Genetic Engineering and Biotechnology Research Institute, Sadat City University, Sadat, Egypt.
Jazyk:	angličtina
Zdroj:	Infectious disorders drug targets [Infect Disord Drug Targets] 2019; Vol. 19 (1), pp. 55-66.
DOI:	10.2174/1871526518666171215123214
Abstrakt:	Background: The p7-transactivated protein1 of Hepatitis C virus is a small integral membrane protein of 127 amino acids, which is crucial for assembly and release of infectious virions. Ab initio or comparative modelling, is an essential tool to solve the problem of protein structure prediction and to comprehend the physicochemical fundamental of how proteins fold in nature. Results: Only one domain (1-127) of p7-transactivated protein1 has been predicted using the systematic in silico approach, ThreaDom. I-TASSER was ranked as the best server for full-length 3-D protein structural predictions of p7-transactivated protein1 where the benchmarked scoring system such as C-score, TM-score, RMSD and Z-score are used to obtain quantitative assessments of the I-TASSER models. Scanning protein motif databases, along with secondary and surface accessibility predictions integrated with post translational modification sites (PTMs) prediction revealed functional and protein binding motifs. Three protein binding motifs (two Asp/Glutamnse, CTNNB1- bd_N) with high sequence conservation and two PTMs prediction: Camp_phospho_site and Myristyl site were predicted using BLOCKS and PROSITE scan. These motifs and PTMs were related to the function of p7-transactivated protein1 protein in inducing ion channel/pore and release of infectious virions. Using SCOP, only one hit matched protein sequence at 71-120 was classified as small proteins and FYVE/PHD zinc finger superfamily. Conclusion: Integrating this information about the p7-transactivated protein1 with SCOP and CATH annotations of the templates facilitates the assignment of structure-function/ evolution relationships to the known and the newly determined protein structures. (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)
Databáze:	MEDLINE
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