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VENN, a tool for titrating sequence conservation onto protein structures.
Vyas, Jay; Gryk, Michael R; Schiller, Martin R.
Afiliação
  • Vyas J; Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030-3305, USA.
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/.
Assuntos

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

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