Open AccessInteraction model between quercetin (3,5,7,3p,4p-pentahidroxiflavone) and human shock thermic factor (HFS)
Author(s) -
B Diana Carolina Clavijo,
R Juvenal Yosa,
S Orlando Acevedo,
Claudia Cifuentes,
Carlos M Estévez Bretón
Publication year - 2017
Publication title -
cuarzo/revista cuarzo
Language(s) - English
Resource type - Journals
eISSN - 2500-7181
pISSN - 0121-2133
DOI - 10.26752/cuarzo.v22.n2.164
Subject(s) - quercetin , trimer , kluyveromyces lactis , docking (animal) , transcription factor , homology modeling , chemistry , heat shock protein , microbiology and biotechnology , biology , biochemistry , dimer , gene , medicine , enzyme , nursing , organic chemistry , antioxidant , saccharomyces cerevisiae
. The expression of the HSP stress inducted are regulated by the Shock Thermic Factor (HSF), that exists in an inactive form as a monomer and when it becomes a trimer can make a bind to DNA activating the HSP transcription.OBJECTIVE. Design a computational model that helps elucidate possible interactions between quercetin fl avonoid and proteins such as HSF-1.METHODOLOGY. To observe how the quercetin possibly affects the timerization of HFS, we make an homology model of the human shock factor (HFS-1), obtaining a high structural homology model with the same protein in Kluyveromyces lactis, this model was used to make docking with the fl avonoid quercetin ( 3,5,7,3p,4p-pentahidroxifl avone).RESULTS AND CONCLUSION. The doking result shows that the quercetin docks to a loop (wing), that is important in the protein-protein interaction, possibly affecting they’re trimerization.