title: Intrinsically disordered proteins in bcl-2 regulated apoptosis.
abstract: Intrinsic cell death is mediated by interaction between pro-apoptotic and pro-survival proteins of the B-cell lymphoma-2 (Bcl-2) family. Members of this family are either intrinsically disordered or contain intrinsically disordered regions/domains that are critical to their function. Alternate splicing and post-translational modifications can determine the extent of these disordered regions and are critical for regulating Bcl-2 proteins. Conformational plasticity and structural transitions characterize the interactions within the Bcl-2 family, with conserved sequence motifs on both binding partners required for their molecular recognition.
authors.affiliation: Walter and Eliza Hall Institute of Medical Research, Parkville, Australia.
authors.forename: Gilles J P
authors.initials: GJ
authors.lastname: Rautureau
authors.forename: Catherine L
authors.initials: CL
authors.lastname: Day
authors.forename: Mark G
authors.initials: MG
authors.lastname: Hinds
mesh_terms: D017398:Alternative Splicing; D017209:Apoptosis; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000737:chemistry / Q000378:metabolism*
chemical_list: D064267:Intrinsically Disordered Proteins; D019253:Proto-Oncogene Proteins c-bcl-2