Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs
The target of rapamycin (TOR), also known as FKBP-rapamycin associated protein (FRAP), is a protein kinase belonging to the PIKK (phosphatidylinositol 3-kinase (PI3K)-related kinases) family. TOR kinases are involved in several signaling pathways that control cell growth and proliferation. <i>...
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MDPI AG
2021-07-01
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| Series: | Genes |
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| Online Access: | https://www.mdpi.com/2073-4425/12/8/1139 |
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| author | Patricia L. A. Muñoz-Muñoz Rosa E. Mares-Alejandre Samuel G. Meléndez-López Marco A. Ramos-Ibarra |
| author_facet | Patricia L. A. Muñoz-Muñoz Rosa E. Mares-Alejandre Samuel G. Meléndez-López Marco A. Ramos-Ibarra |
| author_sort | Patricia L. A. Muñoz-Muñoz |
| collection | DOAJ |
| description | The target of rapamycin (TOR), also known as FKBP-rapamycin associated protein (FRAP), is a protein kinase belonging to the PIKK (phosphatidylinositol 3-kinase (PI3K)-related kinases) family. TOR kinases are involved in several signaling pathways that control cell growth and proliferation. <i>Entamoeba histolytica</i>, the protozoan parasite that causes human amoebiasis, contains two genes encoding TOR-like proteins: <i>Eh</i>FRAP and <i>Eh</i>TOR2. To assess their potential as drug targets to control the cell proliferation of <i>E. histolytica</i>, we studied the structural features of <i>Eh</i>FRAP and <i>Eh</i>TOR2 using a biocomputational approach. The overall results confirmed that both TOR amoebic homologs share structural similarities with functional TOR kinases, and show inherent abilities to form TORC complexes and participate in protein-protein interaction networks. To our knowledge, this study represents the first in silico characterization of the structure-function relationships of <i>Eh</i>FRAP and <i>Eh</i>TOR2. |
| first_indexed | 2024-03-10T08:48:09Z |
| format | Article |
| id | doaj.art-d3b3f265edf44c15b0c92dde5f408918 |
| institution | Directory Open Access Journal |
| issn | 2073-4425 |
| language | English |
| last_indexed | 2024-03-10T08:48:09Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Genes |
| spelling | doaj.art-d3b3f265edf44c15b0c92dde5f4089182023-11-22T07:45:10ZengMDPI AGGenes2073-44252021-07-01128113910.3390/genes12081139Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional HomologsPatricia L. A. Muñoz-Muñoz0Rosa E. Mares-Alejandre1Samuel G. Meléndez-López2Marco A. Ramos-Ibarra3Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoBiotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoThe target of rapamycin (TOR), also known as FKBP-rapamycin associated protein (FRAP), is a protein kinase belonging to the PIKK (phosphatidylinositol 3-kinase (PI3K)-related kinases) family. TOR kinases are involved in several signaling pathways that control cell growth and proliferation. <i>Entamoeba histolytica</i>, the protozoan parasite that causes human amoebiasis, contains two genes encoding TOR-like proteins: <i>Eh</i>FRAP and <i>Eh</i>TOR2. To assess their potential as drug targets to control the cell proliferation of <i>E. histolytica</i>, we studied the structural features of <i>Eh</i>FRAP and <i>Eh</i>TOR2 using a biocomputational approach. The overall results confirmed that both TOR amoebic homologs share structural similarities with functional TOR kinases, and show inherent abilities to form TORC complexes and participate in protein-protein interaction networks. To our knowledge, this study represents the first in silico characterization of the structure-function relationships of <i>Eh</i>FRAP and <i>Eh</i>TOR2.https://www.mdpi.com/2073-4425/12/8/1139target of rapamycinFKBP-rapamycin associated proteinhomology-based protein modelingstructure-function biocomputational analysis<i>Entamoeba histolytica</i> |
| spellingShingle | Patricia L. A. Muñoz-Muñoz Rosa E. Mares-Alejandre Samuel G. Meléndez-López Marco A. Ramos-Ibarra Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs Genes target of rapamycin FKBP-rapamycin associated protein homology-based protein modeling structure-function biocomputational analysis <i>Entamoeba histolytica</i> |
| title | Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs |
| title_full | Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs |
| title_fullStr | Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs |
| title_full_unstemmed | Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs |
| title_short | Bioinformatic Analysis of Two TOR (Target of Rapamycin)-Like Proteins Encoded by <i>Entamoeba histolytica</i> Revealed Structural Similarities with Functional Homologs |
| title_sort | bioinformatic analysis of two tor target of rapamycin like proteins encoded by i entamoeba histolytica i revealed structural similarities with functional homologs |
| topic | target of rapamycin FKBP-rapamycin associated protein homology-based protein modeling structure-function biocomputational analysis <i>Entamoeba histolytica</i> |
| url | https://www.mdpi.com/2073-4425/12/8/1139 |
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