title: Fine-tuning ER-beta structure with PTMs.
abstract: Estrogen receptor beta is differentially regulated by alternative O-GlcNAcylation/O-phosphorylation at Ser(16). NMR, CD, and molecular dynamics analyses of model peptides show that these alternative modifications induce different peptide conformations, providing a molecular basis for their differential regulation of protein function.
authors.affiliation: Department of Biological Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, USA.
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
authors.forename: Kaoru
authors.initials: K
authors.lastname: Sakabe
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism; D000818:Animals; D002942:Circular Dichroism; D047629:Estrogen Receptor beta / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
chemical_list: D047629:Estrogen Receptor beta; D010455:Peptides; D000117:Acetylglucosamine