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

• Published in: International journal of molecular sciences 2023-07, Vol.24 (15), p.11992
• Main Authors: Muñoz-Muñoz, Patricia L A, Mares-Alejandre, Rosa E, Meléndez-López, Samuel G, Ramos-Ibarra, Marco A
• Format: Article
• Language: English
• Subjects: Binding sites; Bioinformatics; Biology; Cell growth; Communication; Drugs; Giardia lamblia; Giardia lamblia - metabolism; Giardiasis; Humans; Infectious diseases; Kinases; Ligands; Mechanistic Target of Rapamycin Complex 2 - metabolism; Parasites; Proteins; Protozoa; Signal Transduction; Sirolimus - pharmacology; structure–function computational analysis; target of rapamycin; template-based protein modeling; TOR Serine-Threonine Kinases - metabolism
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms241511992

TOR proteins, also known as targets of rapamycin, are serine/threonine kinases involved in various signaling pathways that regulate cell growth. The protozoan parasite 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 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 cell proliferation. Furthermore, our study represents a step toward rational drug design for specific anti-giardiasis therapeutic agents.