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Molecular modeling studies demonstrate key mutations that could affect the ligand recognition by influenza AH1N1 neuraminidase

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dc.contributor.author Ramirez-Salinas, Gema L.
dc.contributor.author Garcia-Machorro, J.
dc.contributor.author Quiliano, Miguel
dc.contributor.author Zimic, Mirko
dc.contributor.author Briz, Veronica
dc.contributor.author Rojas-Hernandez, Saul
dc.contributor.author Correa-Basurto, J.
dc.date.accessioned 2019-02-06T14:52:40Z
dc.date.available 2019-02-06T14:52:40Z
dc.date.issued 2015
dc.identifier.uri https://hdl.handle.net/20.500.12866/5353
dc.description.abstract The goal of this study was to identify neuraminidase (NA) residue mutants from human influenza AH1N1 using sequences from 1918 to 2012. Multiple alignment studies of complete NA sequences (5732) were performed. Subsequently, the crystallographic structure of the 1918 influenza (PDB ID: 3BEQ-A) was used as a wild-type structure and three-dimensional (3-D) template for homology modeling of the mutated selected NA sequences. The 3-D mutated NAs were refined using molecular dynamics (MD) simulations (50 ns). The refined 3-D models were used to perform docking studies using oseltamivir. Multiple sequence alignment studies showed seven representative mutations (A232V, K262R, V263I, T264V, S367L, S369N, and S369K). MD simulations applied to 3-D NAs showed that each NA had different active-site shapes according to structural surface visualization and docking results. Moreover, Cartesian principal component analyses (cPCA) show structural differences among these NA structures caused by mutations. These theoretical results suggest that the selected mutations that are located outside of the active site of NA could affect oseltamivir recognition and could be associated with resistance to oseltamivir. en_US
dc.language.iso eng
dc.publisher Springer
dc.relation.ispartof urn:issn:0948-5023
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject Amino Acid Sequence en_US
dc.subject Protein Structure, Tertiary en_US
dc.subject Mutations en_US
dc.subject Principal Component Analysis en_US
dc.subject Models, Molecular en_US
dc.subject Binding Sites en_US
dc.subject Docking en_US
dc.subject Influenza A H1N1 en_US
dc.subject Influenza A Virus, H1N1 Subtype/enzymology en_US
dc.subject Ligands en_US
dc.subject Molecular Docking Simulation en_US
dc.subject Molecular Dynamics Simulation en_US
dc.subject Molecular dynamics simulations en_US
dc.subject Neuraminidase en_US
dc.subject Neuraminidase/chemistry en_US
dc.subject Point Mutation en_US
dc.subject Viral Proteins/chemistry en_US
dc.title Molecular modeling studies demonstrate key mutations that could affect the ligand recognition by influenza AH1N1 neuraminidase en_US
dc.type info:eu-repo/semantics/article
dc.identifier.doi https://doi.org/10.1007/s00894-015-2835-6
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#3.02.00 es_PE
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#1.06.03


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