PUTATIVE DIMERIC ORGANIZATION OF NUCLEAR RECEPTOR HORMONE-BINDING DOMAINS, DEDUCED FROM HYDROPHOBIC CLUSTER-ANALYSIS

2D hydrophobic cluster annlysis (HCA) protein sequence processing, eff icient 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) f old, previously proposed, is confirmed as a likely framework for the h ormone-binding domain and leads to a logical dimerization. Furthermore , homo- or hetero-dimerization creates sites where hormone could likel y be bound, itself being an active component of the dimerization. This model fulfils many of the biochemcial and biological data.