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

Abstract:

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 completely abrogated AR LBD interaction. Strong interactions were still observed followin...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m602567200

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Journal:
Journal of biological chemistry
Volume:
281
Issue:
28
Pages:
19407-19416
Publication date:
2006-07-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
284893

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