Molecular interactions between monoclonal oligomer-specific antibody 5E3 and its amyloid beta cognates
Fig 4
A) Top-ranked docked structure of Fv5E3 and the trimer by Kreutzer et al. The stick and solvent-exposed surface representations of the K28 residue of chain B of the trimer and the E102 of the heavy chain of Fv5E3 are shown in yellow and orange colors, respectively. B) Complex after 100 ns of MD simulation. C) The LRMSD of Cα atoms of the complex (red), Fv5E3 (black), and the oligomer (blue) during the 100-ns MD simulation. D) Top-ranked docked structure of Fv5E3 and the tetramer model of AβOs by Streltsov et al. The stick and solvent-exposed surface representations of the K28 residue of the chain D of the tetramer, and the E102 residue of the heavy chain of Fv5E3 are shown in yellow and red, respectively. Chain E is shown in orange. E) Complex after 100 ns of MD simulation. F) The LRMSD of Cα atoms of the complex (red), Fv5E3 (black), and the tetramer (blue) during the 100 ns MD simulation. G) Top-ranked docked structure of Fv5E3 and the octadecamer by Gu et al. The chains that are close to Fv5E3 are shown in various colors. H) Complex after 100 ns of MD simulation. I) The LRMSD of Cα atoms of the complex (red), Fv5E3 (black), and the prefibrillar oligomer (blue) during the 100 ns MD simulation.