N-Glycosylation as determinant of epidermal growth factor receptor conformation in membranes.

ABSTRACT: The epidermal growth factor receptor (EGFR) regulates several critical cellular processes and is an important target for cancer therapy. In lieu of a crystallographic structure of the complete receptor, atomistic molecular dynamics (MD) simulations have recently shown that they can excel in studies of the full-length receptor. Here we present atomistic MD simulations of the monomeric N-glycosylated human EGFR in biomimetic lipid bilayers that are, in parallel, also used for the reconstitution of full-length receptors. This combination enabled us to experimentally validate our simulations, using ligand binding assays and antibodies to monitor the conformational properties of the receptor reconstituted into membranes. We find that N-glycosylation is a critical determinant of EGFR conformatio

SUBMITTER: Kaszuba K 

PROVIDER: S-EPMC4394299 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature