Title : Allosteric interactions prime androgen receptor dimerization and activation.

Pub. Date : 2022 Jun 2

PMID : 35447082






2 Functional Relationships(s)
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1 Using single-particle cryo-electron microscopy, we isolated three conformations of AR bound to DNA, showing that AR forms a non-obligate dimer, with the buried dimer interface utilized by ancestral steroid receptors repurposed to facilitate cooperative DNA binding. Steroids androgen receptor Homo sapiens
2 Using single-particle cryo-electron microscopy, we isolated three conformations of AR bound to DNA, showing that AR forms a non-obligate dimer, with the buried dimer interface utilized by ancestral steroid receptors repurposed to facilitate cooperative DNA binding. Steroids androgen receptor Homo sapiens