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Article

Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain.

The Journal of biological chemistry - 14 Jul 2006

van de Wijngaart Dennis J, van Royen Martin E, Hersmus Remko, Pike Ashley C W, Houtsmuller Adriaan B, Jenster Guido, Trapman Jan, Dubbink Hendrikus J

Abstract excerpt

Upon hormone binding, a hydrophobic coactivator binding groove is induced in the androgen receptor (AR) ligand-binding domain (LBD). This groove serves as high affinity docking site for alpha-helical FXXLF motifs present in the AR N-terminal domain and in AR cofactors. Study of the amino acid requirements at position +4 of the AR FXXLF motif revealed that most amino acid substitutions strongly reduced or...

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PMID: 16690616
DOI: 10.1074/jbc.M602567200

Genes

PAK6

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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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