Cargando…

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

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 bioinformat...

Descripción completa

Detalles Bibliográficos
Autores principales: Muñoz-Muñoz, Patricia L. A., Mares-Alejandre, Rosa E., Meléndez-López, Samuel G., Ramos-Ibarra, Marco A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10418948/
https://www.ncbi.nlm.nih.gov/pubmed/37569368
http://dx.doi.org/10.3390/ijms241511992
_version_ 1785088391650476032
author Muñoz-Muñoz, Patricia L. A.
Mares-Alejandre, Rosa E.
Meléndez-López, Samuel G.
Ramos-Ibarra, Marco A.
author_facet Muñoz-Muñoz, Patricia L. A.
Mares-Alejandre, Rosa E.
Meléndez-López, Samuel G.
Ramos-Ibarra, Marco A.
author_sort Muñoz-Muñoz, Patricia L. A.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-10418948
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-104189482023-08-12 Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach Muñoz-Muñoz, Patricia L. A. Mares-Alejandre, Rosa E. Meléndez-López, Samuel G. Ramos-Ibarra, Marco A. Int J Mol Sci Communication 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. MDPI 2023-07-26 /pmc/articles/PMC10418948/ /pubmed/37569368 http://dx.doi.org/10.3390/ijms241511992 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Communication
Muñoz-Muñoz, Patricia L. A.
Mares-Alejandre, Rosa E.
Meléndez-López, Samuel G.
Ramos-Ibarra, Marco A.
Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach
title Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach
title_full Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach
title_fullStr Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach
title_full_unstemmed Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach
title_short Structural Insights into the Giardia lamblia Target of Rapamycin Homolog: A Bioinformatics Approach
title_sort structural insights into the giardia lamblia target of rapamycin homolog: a bioinformatics approach
topic Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10418948/
https://www.ncbi.nlm.nih.gov/pubmed/37569368
http://dx.doi.org/10.3390/ijms241511992
work_keys_str_mv AT munozmunozpatriciala structuralinsightsintothegiardialambliatargetofrapamycinhomologabioinformaticsapproach
AT maresalejandrerosae structuralinsightsintothegiardialambliatargetofrapamycinhomologabioinformaticsapproach
AT melendezlopezsamuelg structuralinsightsintothegiardialambliatargetofrapamycinhomologabioinformaticsapproach
AT ramosibarramarcoa structuralinsightsintothegiardialambliatargetofrapamycinhomologabioinformaticsapproach