Fine-Tuning ER-β Structure with PTMs

Gerald Warren Hart, Kaoru Sakabe

Research output: Contribution to journalArticle

Abstract

Estrogen receptor β is differentially regulated by alternative O-GlcNAcylation/O-phosphorylation at Ser16. NMR, CD, and molecular dynamics analyses of model peptides [1] show that these alternative modifications induce different peptide conformations, providing a molecular basis for their differential regulation of protein function.

Original languageEnglish (US)
Pages (from-to)923-924
Number of pages2
JournalChemistry and Biology
Volume13
Issue number9
DOIs
StatePublished - Sep 2006

Fingerprint

Pulse time modulation
Tuning
Peptides
Phosphorylation
Molecular Dynamics Simulation
Estrogen Receptors
Conformations
Molecular dynamics
Nuclear magnetic resonance
Proteins

ASJC Scopus subject areas

  • Organic Chemistry

Cite this

Fine-Tuning ER-β Structure with PTMs. / Hart, Gerald Warren; Sakabe, Kaoru.

In: Chemistry and Biology, Vol. 13, No. 9, 09.2006, p. 923-924.

Research output: Contribution to journalArticle

Hart, Gerald Warren ; Sakabe, Kaoru. / Fine-Tuning ER-β Structure with PTMs. In: Chemistry and Biology. 2006 ; Vol. 13, No. 9. pp. 923-924.
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