Accession Number : ADA320055
Title : Structure/Function of Recombinant Human Estrogen Receptor.
Descriptive Note : Annual rept. 1 Sep 95-31 Aug 96,
Corporate Author : CALIFORNIA UNIV IRVINE
Personal Author(s) : Vickery, Larry E.
PDF Url : ADA320055
Report Date : SEP 1996
Pagination or Media Count : 31
Abstract : Interaction of the estrogen receptor with its ligands is mediated by a C-terminal region of the protein designated the hormone binding domain (HBD) and residues within the HBD are thought to contribute to dimerization. To examine dimer interactions in the isolated HBD, a human estrogen receptor HBD fragment was expressed in high yield as a cleavable fusion protein in Escherichia coli. The isolated estrogen receptor HBD dimerizes and undergoes conformational changes associated with cooperative ligand binding in a manner comparable to the full-length protein, that the N-terminus of the HBD contributes to dimer interactions, and that one effect of ligand binding is to alter the dissociation kinetics of the receptor protein dimer. Current progress includes determination of ligand binding stoichiometry, development of an assay for examining dimer dissociation kinetics in solution, and construction and screening of several mutant proteins.
Descriptors : *HUMANS, *ESTROGENS, *BREAST CANCER, FUNCTIONS, HORMONES, INTERACTIONS, PROTEINS, ISOLATION, MUTATIONS, ESCHERICHIA COLI, PURIFICATION, LIGANDS, GENES, KINETICS, MUTAGENS, DISSOCIATION, ASSAYING, STOICHIOMETRY, SENSE ORGANS, RECEPTOR SITES(PHYSIOLOGY), DIMERS, STEROIDS.
Subject Categories : Biochemistry
Genetic Engineering and Molecular Biology
Medicine and Medical Research
Distribution Statement : APPROVED FOR PUBLIC RELEASE