Antibody binding modulates the dynamics of the membrane-bound prion protein.

ABSTRACT: Misfolding of the cellular prion protein (PrP^C) is associated with lethal neurodegeneration. PrP^C consists of a flexible tail (residues 23-123) and a globular domain (residues 124-231) whose C-terminal end is anchored to the cell membrane. The neurotoxic antibody POM1 and the innocuous antibody POM6 recognize the globular domain. Experimental evidence indicates that POM1 binding to PrP^C emulates the influence on PrP^C of the misfolded prion protein (PrP^Sc) while the binding of POM6 has the opposite biological response. Little is known about the potential interactions between flexible tail, globular domain, and the membrane. Here, we used atomistic simulations to investigate how these interactions are modulated by the binding of the Fab

SUBMITTER: Ilie IM 

PROVIDER: S-EPMC9382331 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature