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Article

Mutations of tyrosine 537 in the human estrogen receptor-alpha selectively alter the receptor's affinity for estradiol and the kinetics of the interaction.

Biochemistry - 2 Apr 2002

Zhong L, Skafar D F

Abstract excerpt

Mutation of tyrosine 537 (Y537) of the human estrogen receptor-alpha (hERalpha) produces receptors having a range of constitutive activity, which suggests that this residue modulates the conformational changes of the receptor. We investigated the effect of several mutations at this position, to phenylalanine (Y537F), to serine (Y537S), and to glutamic acid (Y537E), on the hormone-binding properties of the...

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Identifiers

PMID: 11914066
DOI: 10.1021/bi0121095

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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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