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Title

 

 

 

 

 

Insights from the analysis of a predicted model of gp63 in Leishmania donovani

 

Authors

 

Ali Razzazan1, *, Mohammad Reza Saberi2 and Mahmoud Reza Jaafari3

 

Affiliation

 

 

1Department of Medical Physics and Engineering, School of Medicine, Shahid Beheshti University, M. C., Tehran, Iran; 2Department of Medicinal Chemistry, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran; 3Department of Pharmaceutics, School of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran

 

Email

 

arazzazan@yahoo.com; * Corresponding author

 

Article Type

 

Web Server

 

Date

 

 

received August 28, 2008; accepted September 13, 2008; published November 02,

2008

 

Abstract

Leishmaniasis is a protozoal disease of human that occurs in most parts of the world. By considering the progress of bioinformatics in molecular modeling, major surface glycoprotein of Leishmania donovani (gp63) structure was modeled using homology modeling with high accuracy based on the X-ray crystal structure of the Leishmania major gp63 as a template, and then analyzed 3D structure of gp63 which can reveal exact facts about its structure and interaction. The objective of this study was to find folding and three dimensional structure of the gp63 as potent antigen for human. In this project, we applied the theory of evolution method, including comparative modeling and threading. This study presented a simple protocol for rapid and precise finding 3D structure of gp63 and investigation of its structural properties. The translated amino acid sequence showed that Leishmania donovani gp63 contains 590 amino acids precursor protein consisting of an NH2-terminal signal peptide of 39 amino acids for membrane targeting, a pro region of 48 amino acids, the mature protein of 478 amino acids containing glycosylation and putative catalytic sites, and a COOH-terminal signal peptide of 25 amino acids for GPI attachment. Based on our model, the protein consists of three domains: the N-terminal, central and C-terminal domains. Additionally, these results could guide future structure-function analyses of gp63 protein.

 

Keywords

 

Leishmaniasis; Leishmania donovani; gp63; homology modeling; comparative modeling; 3D structure analysis

 

Citation

 

Razzazan et al., Bioinformation 3(3): 114-118 (2008)

 

Edited by

 

P. Kangueane

 

ISSN

 

0973-2063

 

Publisher

 

Biomedical Informatics

 

License

 

 

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.