Unknown

Dataset Information

0

PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery.


ABSTRACT: 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/.

SUBMITTER: Garcia-Boronat M 

PROVIDER: S-EPMC2447719 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

PVS: a web server for protein sequence variability analysis tuned to facilitate conserved epitope discovery.

Garcia-Boronat Maria M   Diez-Rivero Carmen M CM   Reinherz Ellis L EL   Reche Pedro A PA  

Nucleic acids research 20080427 Web Server issue


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-st  ...[more]

Similar Datasets

| S-EPMC3573977 | biostudies-literature
| S-EPMC6030882 | biostudies-literature
| S-EPMC3125773 | biostudies-literature
| S-EPMC8769915 | biostudies-literature
| S-EPMC4987934 | biostudies-literature
| S-EPMC4086118 | biostudies-literature
| S-EPMC5860439 | biostudies-literature
| S-EPMC1538777 | biostudies-literature
| S-EPMC4086088 | biostudies-literature
| S-EPMC1933189 | biostudies-literature