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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.
Afiliação
  • Gogovi GK; Center for Simulation and Modeling, George Mason University, 4400 University Drive, MSN 6A12, Fairfax, VA 22030, USA. ggogovi@masonlive.gmu.edu.
  • Almsned F; Department of Computational and Data Sciences, George Mason University, 4400 University Drive, MSN 6A12, Fairfax, VA 22030, USA. ggogovi@masonlive.gmu.edu.
  • Bracci N; School of Systems Biology, George Mason University, 10900 University Blvd., MSN 5B3, Manassas, VA 20110, USA. falmsned@masonlive.gmu.edu.
  • Kehn-Hall K; School of Systems Biology, George Mason University, 10900 University Blvd., MSN 5B3, Manassas, VA 20110, USA. nbracci@masonlive.gmu.edu.
  • Shehu A; National Center for Biodefense and Infectious Diseases, George Mason University, 10650 Pyramid Place, MS 1J5, Manassas, VA 20110, USA. nbracci@masonlive.gmu.edu.
  • Blaisten-Barojas E; School of Systems Biology, George Mason University, 10900 University Blvd., MSN 5B3, Manassas, VA 20110, USA. kkehnhal@gmu.edu.
Molecules ; 24(9)2019 May 07.
Article em En | MEDLINE | ID: mdl-31067727
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Febre do Vale de Rift / Vírus da Febre do Vale do Rift / Proteínas Virais / Estrutura Terciária de Proteína Limite: Animals / Humans Idioma: En Revista: Molecules Assunto da revista: BIOLOGIA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Febre do Vale de Rift / Vírus da Febre do Vale do Rift / Proteínas Virais / Estrutura Terciária de Proteína Limite: Animals / Humans Idioma: En Revista: Molecules Assunto da revista: BIOLOGIA Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Estados Unidos