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Biomed Res Int ; 2016: 1674580, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-27294109

RESUMO

The RABVG ectodomain is a homotrimer, and trimers are often called spikes. They are responsible for the attachment of the virus through the interaction with nicotinic acetylcholine receptors, neural cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR). This makes them relevant in viral pathogenesis. The antigenic structure differs significantly between the trimers and monomers. Surfaces rich in hydrophobic amino acids are important for trimer stabilization in which the C-terminal of the ectodomain plays an important role; to understand these interactions between the G proteins, a mechanistic study of their functions was performed with a molecular model of G protein in its trimeric form. This verified its 3D conformation. The molecular modeling of G protein was performed by a I-TASSER server and was evaluated via a Rachamandran plot and ERRAT program obtained 84.64% and 89.9% of the residues in the favorable regions and overall quality factor, respectively. The molecular dynamics simulations were carried out on RABVG trimer at 310 K. From these theoretical studies, we retrieved the RMSD values from Cα atoms to assess stability. Preliminary model of G protein of rabies virus stable at 12 ns with molecular dynamics was obtained.


Assuntos
Antígenos Virais/química , Glicoproteínas/química , Imageamento Tridimensional/métodos , Vírus da Raiva , Proteínas do Envelope Viral/química , Algoritmos , Antígeno CD56/química , Sistema Imunitário , Simulação de Dinâmica Molecular , Proteínas do Tecido Nervoso/química , Domínios Proteicos , Multimerização Proteica , Estrutura Secundária de Proteína , Receptores de Fator de Crescimento Neural/química
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