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Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach

Authors :
Patricia L. A. Muñoz-Muñoz
Rosa E. Mares-Alejandre
Samuel G. Meléndez-López
Marco A. Ramos-Ibarra
Source :
International Journal of Molecular Sciences, Vol 24, Iss 15, p 11992 (2023)
Publication Year :
2023
Publisher :
MDPI AG, 2023.

Abstract

TOR proteins, also known as targets of rapamycin, are serine/threonine kinases involved in various signaling pathways that regulate cell growth. The protozoan parasite Giardia lamblia is the causative agent of giardiasis, a neglected infectious disease in humans. In this study, we used a bioinformatics approach to examine the structural features of GTOR, a G. lamblia TOR-like protein, and predict functional associations. Our findings confirmed that it shares significant similarities with functional TOR kinases, including a binding domain for the FKBP-rapamycin complex and a kinase domain resembling that of phosphatidylinositol 3-kinase-related kinases. In addition, it can form multiprotein complexes such as TORC1 and TORC2. These results provide valuable insights into the structure–function relationship of GTOR, highlighting its potential as a molecular target for controlling G. lamblia cell proliferation. Furthermore, our study represents a step toward rational drug design for specific anti-giardiasis therapeutic agents.

Details

Language :
English
ISSN :
14220067, 16616596, and 96544775
Volume :
24
Issue :
15
Database :
Directory of Open Access Journals
Journal :
International Journal of Molecular Sciences
Publication Type :
Academic Journal
Accession number :
edsdoj.6ec3d71fe7c6453f9654477556723c7a
Document Type :
article
Full Text :
https://doi.org/10.3390/ijms241511992