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VENN, a tool for titrating sequence conservation onto protein structures

Residue conservation is an important, established method for inferring protein function, modularity and specificity. It is important to recognize that it is the 3D spatial orientation of residues that drives sequence conservation. Considering this, we have built a new computational tool, VENN that a...

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Detalles Bibliográficos
Autores principales: Vyas, Jay, Gryk, Michael R., Schiller, Martin R.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764419/
https://www.ncbi.nlm.nih.gov/pubmed/19656955
http://dx.doi.org/10.1093/nar/gkp616
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author Vyas, Jay
Gryk, Michael R.
Schiller, Martin R.
author_facet Vyas, Jay
Gryk, Michael R.
Schiller, Martin R.
author_sort Vyas, Jay
collection PubMed
description Residue conservation is an important, established method for inferring protein function, modularity and specificity. It is important to recognize that it is the 3D spatial orientation of residues that drives sequence conservation. Considering this, we have built a new computational tool, VENN that allows researchers to interactively and graphically titrate sequence homology onto surface representations of protein structures. Our proposed titration strategies reveal critical details that are not readily identified using other existing tools. Analyses of a bZIP transcription factor and receptor recognition of Fibroblast Growth Factor using VENN revealed key specificity determinants. Weblink: http://sbtools.uchc.edu/venn/.
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spelling pubmed-27644192009-10-20 VENN, a tool for titrating sequence conservation onto protein structures Vyas, Jay Gryk, Michael R. Schiller, Martin R. Nucleic Acids Res Methods Online Residue conservation is an important, established method for inferring protein function, modularity and specificity. It is important to recognize that it is the 3D spatial orientation of residues that drives sequence conservation. Considering this, we have built a new computational tool, VENN that allows researchers to interactively and graphically titrate sequence homology onto surface representations of protein structures. Our proposed titration strategies reveal critical details that are not readily identified using other existing tools. Analyses of a bZIP transcription factor and receptor recognition of Fibroblast Growth Factor using VENN revealed key specificity determinants. Weblink: http://sbtools.uchc.edu/venn/. Oxford University Press 2009-10 2009-08-05 /pmc/articles/PMC2764419/ /pubmed/19656955 http://dx.doi.org/10.1093/nar/gkp616 Text en © 2009 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Methods Online
Vyas, Jay
Gryk, Michael R.
Schiller, Martin R.
VENN, a tool for titrating sequence conservation onto protein structures
title VENN, a tool for titrating sequence conservation onto protein structures
title_full VENN, a tool for titrating sequence conservation onto protein structures
title_fullStr VENN, a tool for titrating sequence conservation onto protein structures
title_full_unstemmed VENN, a tool for titrating sequence conservation onto protein structures
title_short VENN, a tool for titrating sequence conservation onto protein structures
title_sort venn, a tool for titrating sequence conservation onto protein structures
topic Methods Online
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2764419/
https://www.ncbi.nlm.nih.gov/pubmed/19656955
http://dx.doi.org/10.1093/nar/gkp616
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