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Article

Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor.

Cell - 23 Mar 1990

Fawell S E, Lees J A, White R, Parker M G

Abstract excerpt

We have identified a region within the steroid binding domain of the mouse estrogen receptor that is required for both receptor dimerization and high affinity DNA binding. Analysis of sequences in this region revealed that a heptad repeat of hydrophobic residues was conserved in all members of the nuclear receptor superfamily. Single amino acid substitutions of residues in the N-terminal half, but not the...

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PMID: 2317866
DOI: 10.1016/0092-8674(90)90343-d

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor.PMID 2317866Read ↗

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Structure and function of the estrogen receptor.Semantic proximity Read ↗

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Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex.Semantic proximity Read ↗

Estrogen receptor α L543A,L544A mutation changes antagonists to agonists, correlating with the ligand binding domain dimerization associated with DNA binding activity.Semantic proximity Read ↗

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