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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...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2009
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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/. |
format | Text |
id | pubmed-2764419 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT vyasjay vennatoolfortitratingsequenceconservationontoproteinstructures AT grykmichaelr vennatoolfortitratingsequenceconservationontoproteinstructures AT schillermartinr vennatoolfortitratingsequenceconservationontoproteinstructures |