title: Structural insights into the Notch-modifying glycosyltransferase Fringe.
abstract: Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo.
authors.affiliation: European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Jinek
authors.forename: Ya-Wen
authors.initials: YW
authors.lastname: Chen
authors.forename: Henrik
authors.initials: H
authors.lastname: Clausen
authors.forename: Stephen M
authors.initials: SM
authors.lastname: Cohen
authors.forename: Elena
authors.initials: E
authors.lastname: Conti
mesh_terms: D000818:Animals; D001665:Binding Sites; D005964:Glucosyltransferases; D016695:Glycosyltransferases / Q000737:chemistry* / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism*; D008274:Magnesium / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D051880:Receptors, Notch / Q000378:metabolism; D013329:Structure-Activity Relationship; D014530:Uridine Diphosphate / Q000737:chemistry
chemical_list: D011506:Proteins; D051880:Receptors, Notch; D014530:Uridine Diphosphate; D016695:Glycosyltransferases; D005964:Glucosyltransferases; C486343:Mfng protein, mouse; D008274:Magnesium