title: Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes.
abstract: Steroid receptors typically exist in a heteromeric complex with Hsp90 and other components of the molecular chaperone machinery. Assembly of functional receptor complexes follows an ordered pathway involving at least eight chaperone components, some only participating in early assembly stages that are prerequisite for formation of mature complexes. The mechanisms directing the order of assembly steps and the nature of transitional interactions between assembly steps are largely unknown, but likely are encoded in the primary sequence and functional domains of the participating chaperones. Several common sequence motifs are shared between participants that may be key in ordering the steroid receptor assembly pathway.
authors.affiliation: Department of Pharmacology, University of Nebraska Medical Center, Omaha 68198-6260, USA.
authors.forename: D F
authors.initials: DF
authors.lastname: Smith
mesh_terms: D000595:Amino Acid Sequence; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011980:Receptors, Progesterone / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
chemical_list: D018832:Molecular Chaperones; D010455:Peptides; D011980:Receptors, Progesterone