Putative dimeric organization of nuclear receptor hormone-binding domains, deduced from hydrophobic cluster analysis.
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.
Mornon
J P
JP
Département des Macromolécules Biologiques, Universités Paris VI/Paris VII, France.
Thoreau
E
E
Rowlands
D
D
Callebaut
I
I
Moreau
G
G
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
D006728:Hormones; D011956:Receptors, Cell Surface; D018160:Receptors, Cytoplasmic and Nuclear; D015843:Serpins