10.5452/MA-AEQ5E
Fernandes, Carlos Alexandre Henrique; Matiolli, Fabio Filippi; Pavani, Raphael Souza; Fontes, Marcos Roberto de Mattos; Elias, Maria Carolina Quartiam
In silico structure of OB-fold domains 1 and 2 of RPA1 from Trypanosoma cruzi docked a single stranded telomeric DNA
modelarchive.org
2018
3D macromolecular model
2018-07-18
en
Replication Protein A (RPA) is the major single-stranded binding protein from eukaryotes. RPA is a conserved heterotrimeric complex composed by subunits RPA-1, RPA-2 and RPA-3 (or RPA70, RPA32 and RPA14, respectively). One of the major structural features of RPA is the presence of the oligonucleotide/oligosaccharide binding (OB) domains within the subunits. Here, we performed docking experiments and molecular dynamics simulations of TcRPA-1-OBF12 in silico model (previously reported at doi: 10.5452/ma-azgkp) with asingle stranded telomeric DNA (TTAGGGTTAG) in order to evaluate protein/DNA interactions.