The role of salt concentration and magnesium binding in HIV-1 subtype-A and subtype-B kissing loop monomer structures.

ABSTRACT: The subtype-B monomers of the human immunodeficiency virus type-1 (HIV-1) have experimentally been shown to dimerize at high salt concentration or in the presence of magnesium, while the dimerization of the subtype-A monomers requires magnesium binding at the G273 or G274 phosphate groups regardless of salt concentration. We used explicit solvent molecular dynamics (MD) simulations to investigate the conformational changes in subtype-A and -B monomers in different salt concentrations, and we found that our MD simulation results are consistent with those of experiments. At low salt concentration, hairpin loop structures of both subtypes were deformed and bases in the hairpin loop were turned inside. At high salt concentrations, the subtype-B monomer maintained the hairpin loop shape and mos

SUBMITTER: Kim T 

PROVIDER: S-EPMC6319921 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature