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Nucleic Acids Res. 2009 Oct;37(18):e124. doi: 10.1093/nar/gkp616. Epub 2009 Aug 5.

VENN, a tool for titrating sequence conservation onto protein structures.

Author information

1
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030-3305, USA.

Abstract

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/.

PMID:
19656955
PMCID:
PMC2764419
DOI:
10.1093/nar/gkp616
[Indexed for MEDLINE]
Free PMC Article

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