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/.
Amino acid sequence; CCAAT-Enhancer-Binding Protein-beta/chemistry; Conserved Sequence; Fibroblast Growth Factor 8/chemistry; Fibroblast growth factors; Fibroblasts; Humans; Models; Molecular; Proteins—Conformation; Protein Conformation; Sequence Homology; Amino Acid; Software
Biology | Computer Sciences | Life Sciences | Molecular Biology | Structural Biology
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Gryk, M. R.,
Schiller, M. R.
VENN, a tool for titrating sequence conservation onto protein structures.
Nucleic Acids Research, 37(18),