VENN, a tool for titrating sequence conservation onto protein structures.
Nucleic Acids Res
; 37(18): e124, 2009 Oct.
Article
em En
| MEDLINE
| ID: mdl-19656955
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/.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Software
/
Homologia de Sequência de Aminoácidos
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Nucleic Acids Res
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Estados Unidos