Exploring electrostatic patterns of human, murine, equine and canine TLR4/MD-2 receptors.

ABSTRACT: Electrostatic interactions between phosphate anions and Toll-like receptor 4 / Myeloid differentiation factor-2 (TLR4/MD-2) protein complexes of human, murine, equine and canine species were computed. Such knowledge can provide mechanistic information about recognising LPS-like ligands, since anionic phosphate groups belong to the structural features of LPS with their diphosphorylated diglucosamine backbone. Sequence composition analyses, electrostatic interaction potentials and docked energies as well as molecular dynamics studies evaluated the phosphate interactions within the triangular LPS binding site (wedge). According to electrostatic analyses, human, horse and dog wedges possess phosphate-binding sites with indistinct positive and negative charge distributions, but the murine wedge

SUBMITTER: Lozano-Aponte J 

PROVIDER: S-EPMC7903528 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature