Skip to content
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
Cloning, expression and dynamic simulation of TRYP6 from Leishmania major (MRHO/IR/75/ER)
Molecular Biology Reports, Volume 38, No. 6, Year 2011
Notification
URL copied to clipboard!
Description
Leishmania, a digenetic protozoan parasite causes severe diseases in human and animals. Efficient evasion of toxic microbicidal molecules, such as reactive oxygen species and reactive nitrogen species is crucial for Leishmania to survive and replicate in the host cells. Tryparedoxin peroxidase, a member of peroxiredoxins family, is vital for parasite survival in the presence of antioxidant, hence it is one of the most important molecules in Leishmania viability and then, it may be an appropriate goal for challenging against leishmaniasis. After cloning and sub-cloning of TRYP6 from Leishmania major (MRHO/IR/75/ER), homology modeling of the LmTRYP6 was proposed to predict some functional property of this protein. The refined model showed that the core structure consists of a seven b stranded b-sheet and five a helices which are organized as a central 7-stranded β2-β1- β5-β4-β3- β6-β7 surrounded by 2-stranded β-hairpin, a helices A and D on one side, and a helices B, C and E on the other side. The peroxidatic active site is located in a pocket formed by the residue Pro45, Met46, Thr49, Val51, Cys52, Arg128, Met147 and Pro 148. The catalytic Cys52, located in the first turn of helix αB, is in van der Waals with a Pro45, a Thr49 and an Arg128 that are absolutely conserved in all known Prx sequences. In this study, an attractive molecular target was studied. These results might be used in designing of drugs to fight an important human pathogen. © Springer Science+Business Media B.V. 2010.
Authors & Co-Authors
Eslami, Gilda
Iran, Yazd
Shahid Sadoughi University of Medical Sciences
Frikha, Fakher
Tunisia, Sfax
Ecole Nationale D'ingénieurs de Sfax
Salehi, Rasoul
Iran, Isfahan
Isfahan University of Medical Sciences
Khamesipour, Ali
Iran, Tehran
Center for Research and Training in Skin Disease and Leprosy Tums
Hejazi, Seyed Hossein
Iran, Isfahan
Isfahan University of Medical Sciences
Nilforoshzadeh, Mohammad Ali
Iran, Isfahan
Skin Diseases and Leishmaniasis Rc, Isfahan Ums
Statistics
Citations: 9
Authors: 6
Affiliations: 5
Identifiers
Doi:
10.1007/s11033-010-0492-5
ISSN:
03014851
e-ISSN:
15734978
Research Areas
Environmental