title: Molecular structure of human geminin.
abstract: The origin licensing repressor geminin is a unique bifunctional protein providing a molecular link between cellular proliferation, differentiation and genomic stability. Here we report the first molecular structure of human geminin, determined by EM and image processing at a resolution of 17.5 A. The geminin molecule is a tetramer formed by two dimers with monomers interacting via coiled-coil domains. The unusual structural organization of geminin provides molecular insight into its bifunctional nature.
authors.affiliation: Bloomsbury Centre of Structural Biology, Birkbeck College, Malet Street, London, WC1E 7HX, UK.
authors.forename: Andrei L
authors.initials: AL
authors.lastname: Okorokov
authors.forename: Elena V
authors.initials: EV
authors.lastname: Orlova
authors.forename: Sarah R
authors.initials: SR
authors.lastname: Kingsbury
authors.forename: Claire
authors.initials: C
authors.lastname: Bagneris
authors.forename: Ulrich
authors.initials: U
authors.lastname: Gohlke
authors.forename: Gareth H
authors.initials: GH
authors.lastname: Williams
authors.forename: Kai
authors.initials: K
authors.lastname: Stoeber
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000648:ultrastructure; D064248:Geminin; D006801:Humans; D008854:Microscopy, Electron; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D018797:Cell Cycle Proteins; C577995:GMNN protein, human; D064248:Geminin