title: Putative dimeric organization of nuclear receptor hormone-binding domains, deduced from hydrophobic cluster analysis.
abstract: 2D hydrophobic cluster analysis (HCA) protein sequence processing, efficient at low levels of sequence identity, leads to a coherent scheme for the structural organization of the hormone-binding domains (HBDs) of nuclear receptors. The typical serine protease inhibitor (serpin) fold, previously proposed, is confirmed as a likely framework for the hormone-binding domain and leads to a logical dimerization. Furthermore, homo- or hetero-dimerization creates sites where hormone could likely be bound, itself being an active component of the dimerization. This model fulfils many of the biochemical and biological data.
authors.affiliation: Département des Macromolécules Biologiques, Universités Paris VI/Paris VII, France.
authors.forename: J P
authors.initials: JP
authors.lastname: Mornon
authors.forename: E
authors.initials: E
authors.lastname: Thoreau
authors.forename: D
authors.initials: D
authors.lastname: Rowlands
authors.forename: I
authors.initials: I
authors.lastname: Callebaut
authors.forename: G
authors.initials: G
authors.lastname: Moreau
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D016000:Cluster Analysis; D006728:Hormones / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure*; D015843:Serpins / Q000648:ultrastructure
chemical_list: D006728:Hormones; D011956:Receptors, Cell Surface; D018160:Receptors, Cytoplasmic and Nuclear; D015843:Serpins