%0 Journal Article
%T Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach.
%A Muñoz-Muñoz PLA
%A Mares-Alejandre RE
%A Meléndez-López SG
%A Ramos-Ibarra MA
%J Int J Mol Sci
%V 24
%N 15
%D 2023 Jul 26
%M 37569368
%F 6.208
%R 10.3390/ijms241511992
%X 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.