Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs

Bin He, Elizabeth M. Wilson

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


Coactivator recruitment by activation function 2 (AF2) in the steroid receptor ligand binding domain takes place through binding of an LXXLL amphipathic α-helical motif at the AF2 hydrophobic surface. The androgen receptor (AR) and certain AR coregulators are distinguished by an FXXLF motif that interacts selectively with the AR AF2 site. Here we show that LXXLL and FXXLF motif interactions with steroid receptors are modulated by oppositely charged residues flanking the motifs and charge clusters bordering AF2 in the ligand binding domain. An increased number of charged residues flanking AF2 in the ligand binding domain complement the two previously characterized charge clamp residues in coactivator recruitment. The data suggest a model whereby coactivator recruitment to the receptor AF2 surface is initiated by complementary charge interactions that reflect a reversal of the acidic activation domain-coactivator interaction model.

Original languageEnglish (US)
Pages (from-to)2135-2150
Number of pages16
JournalMolecular and Cellular Biology
Issue number6
StatePublished - Mar 2003

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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