A molecular modelling study on the hormone binding site of the estrogen receptor.
Using molecular modelling techniques, the structures of ligands with high affinity to the estrogen receptor were investigated. In order to determine the biologically active conformations and orientations within the hormone binding site a comparative study on the basis of molecular shapes and molecular fields was performed. The corresponding pharmacophore provides the basis for an amino acid model of the hormone binding site. Based on this model several experimental data can be understood.
Institut für Pharmazie, Freien Universität, Berlin.
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D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*; D011960:Receptors, Estrogen / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014598:Uteroglobin / Q000737:chemistry / Q000378:metabolism
D011956:Receptors, Cell Surface; D011960:Receptors, Estrogen; D014598:Uteroglobin