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Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein
A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate the structure of the Rift Valley fever virus...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6539450/ https://www.ncbi.nlm.nih.gov/pubmed/31067727 http://dx.doi.org/10.3390/molecules24091768 |
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author | Gogovi, Gideon K. Almsned, Fahad Bracci, Nicole Kehn-Hall, Kylene Shehu, Amarda Blaisten-Barojas, Estela |
author_facet | Gogovi, Gideon K. Almsned, Fahad Bracci, Nicole Kehn-Hall, Kylene Shehu, Amarda Blaisten-Barojas, Estela |
author_sort | Gogovi, Gideon K. |
collection | PubMed |
description | A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate the structure of the Rift Valley fever virus (RVFV) L protein using a combination of in silico techniques. Due to its large size and multiple domains, elucidation of the tertiary structure of the L protein has so far challenged both dry and wet laboratories. In this work, we leverage complementary perspectives and tools from the computational-molecular-biology and bioinformatics domains for constructing, refining, and evaluating several atomistic structural models of the L protein that are physically realistic. All computed models have very flexible termini of about 200 amino acids each, and a high proportion of helical regions. Properties such as potential energy, radius of gyration, hydrodynamics radius, flexibility coefficient, and solvent-accessible surface are reported. Structural characterization of the L protein enables our laboratories to better understand viral replication and transcription via further studies of L protein-mediated protein–protein interactions. While results presented a focus on the RVFV L protein, the following workflow is a more general modeling protocol for discovering the tertiary structure of multidomain proteins consisting of thousands of amino acids. |
format | Online Article Text |
id | pubmed-6539450 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-65394502019-05-31 Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein Gogovi, Gideon K. Almsned, Fahad Bracci, Nicole Kehn-Hall, Kylene Shehu, Amarda Blaisten-Barojas, Estela Molecules Article A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate the structure of the Rift Valley fever virus (RVFV) L protein using a combination of in silico techniques. Due to its large size and multiple domains, elucidation of the tertiary structure of the L protein has so far challenged both dry and wet laboratories. In this work, we leverage complementary perspectives and tools from the computational-molecular-biology and bioinformatics domains for constructing, refining, and evaluating several atomistic structural models of the L protein that are physically realistic. All computed models have very flexible termini of about 200 amino acids each, and a high proportion of helical regions. Properties such as potential energy, radius of gyration, hydrodynamics radius, flexibility coefficient, and solvent-accessible surface are reported. Structural characterization of the L protein enables our laboratories to better understand viral replication and transcription via further studies of L protein-mediated protein–protein interactions. While results presented a focus on the RVFV L protein, the following workflow is a more general modeling protocol for discovering the tertiary structure of multidomain proteins consisting of thousands of amino acids. MDPI 2019-05-07 /pmc/articles/PMC6539450/ /pubmed/31067727 http://dx.doi.org/10.3390/molecules24091768 Text en © 2019 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Gogovi, Gideon K. Almsned, Fahad Bracci, Nicole Kehn-Hall, Kylene Shehu, Amarda Blaisten-Barojas, Estela Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein |
title | Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein |
title_full | Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein |
title_fullStr | Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein |
title_full_unstemmed | Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein |
title_short | Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein |
title_sort | modeling the tertiary structure of the rift valley fever virus l protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6539450/ https://www.ncbi.nlm.nih.gov/pubmed/31067727 http://dx.doi.org/10.3390/molecules24091768 |
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