Abstract
INTRODUCTION. The expression of stress-inducible heat shock proteins (HSPs) is regulated by heat shock factor (HSF), which exists in an inactive monomeric form and upon trimerization is able to bind to DNA and activate HSP transcription.
OBJECTIVE. To design a computational model that contributes to elucidate the possible interactions between the fl avonoid quercetin and proteins such as HSF-1.
METHODOLOGY. To observe how quercetin possibly affects HSF trimerization, the human homology model of the heat shock factor (HSF-1) was performed, obtaining a model with high structural homology with the same protein of Kluyveromyces lactis, this model was used to perform docking with the fl avonoid quercetin (3,5,7,3p,4p-pentahydroxifl avone).
RESULT AND CONCLUSION. The docking result showed that quercetin binds to a loop ("wing"), which is of importance for protein-protein interaction, probably affecting protein-protein trimerization.
OBJECTIVE. To design a computational model that contributes to elucidate the possible interactions between the fl avonoid quercetin and proteins such as HSF-1.
METHODOLOGY. To observe how quercetin possibly affects HSF trimerization, the human homology model of the heat shock factor (HSF-1) was performed, obtaining a model with high structural homology with the same protein of Kluyveromyces lactis, this model was used to perform docking with the fl avonoid quercetin (3,5,7,3p,4p-pentahydroxifl avone).
RESULT AND CONCLUSION. The docking result showed that quercetin binds to a loop ("wing"), which is of importance for protein-protein interaction, probably affecting protein-protein trimerization.
| Translated title of the contribution | Interaction model between quercetin (3,5,7,3p,4p-pentahidroxiflavone) and human shock thermic factor (HFS) |
|---|---|
| Original language | Spanish |
| Pages (from-to) | 73-79 |
| Number of pages | 6 |
| Journal | Revista Cuarzo |
| DOIs | |
| State | Published - Sep 2017 |