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Título:
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PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery.
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Autores:
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García Boronat, María ;
Díez Rivero, Carmen M. ;
Reinherz, Ellis L ;
Reche, Pedro A
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Tipo de documento:
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texto impreso
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Editorial:
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Oxford University Press, 2008
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Dimensiones:
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application/pdf
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Nota general:
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cc_by_nc
info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias Biomédicas: Medicina: Inmunología
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Materia = Ciencias Biomédicas: Biología: Biología molecular
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Materia = Ciencias: Informática: Bioinformática
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Tipo = Artículo
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Resumen:
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We have developed PVS (Protein Variability Server), a web-based tool that uses several variability metrics to compute the absolute site variability in multiple protein-sequence alignments (MSAs). The variability is then assigned to a user-selected reference sequence consisting of either the first sequence in the alignment or a consensus sequence. Subsequently, PVS performs tasks that are relevant for structure-function studies, such as plotting and visualizing the variability in a relevant 3D-structure. Neatly, PVS also implements some other tasks that are thought to facilitate the design of epitope discovery-driven vaccines against pathogens where sequence variability largely contributes to immune evasion. Thus, PVS can return the conserved fragments in the MSA-as defined by a user-provided variability threshold-and locate them in a relevant 3D-structure. Furthermore, PVS can return a variability-masked sequence, which can be directly submitted to the RANKPEP server for the prediction of conserved T-cell epitopes. PVS is freely available at: http://imed.med.ucm.es/PVS/.
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En línea:
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https://eprints.ucm.es/id/eprint/9323/1/34.GarciaB_etal_NAR_2008.pdf
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