title: Mad2 "opens" Cdc20 for BubR1 binding.
abstract: In this issue of Molecular Cell, Han et al. (2013) demonstrate that Mad2 induces a conformational change in Cdc20 that permits BubR1 binding, thereby producing the physiologically relevant APC/C(Cdc20) inhibitor.
authors.affiliation: Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.
authors.forename: Gina V
authors.initials: GV
authors.lastname: Caldas
authors.forename: Jennifer G
authors.initials: JG
authors.lastname: Deluca
mesh_terms: D002135:Calcium-Binding Proteins / Q000502:physiology*; D064199:Cdc20 Proteins; D018797:Cell Cycle Proteins / Q000378:metabolism* / Q000502:physiology*; D006801:Humans; D059566:M Phase Cell Cycle Checkpoints / Q000502:physiology*; D064246:Mad2 Proteins; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012097:Repressor Proteins / Q000502:physiology*
chemical_list: D002135:Calcium-Binding Proteins; D064199:Cdc20 Proteins; D018797:Cell Cycle Proteins; C577697:MAD2L1 protein, human; D064246:Mad2 Proteins; D012097:Repressor Proteins; C577488:CDC20 protein, human; C584277:BUB1 protein, human; C090464:Bub1 spindle checkpoint protein; D017346:Protein Serine-Threonine Kinases