Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain.
van de Wijngaart, Dennis J
Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain. [electronic resource] - The Journal of biological chemistry Jul 2006 - 19407-16 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.M602567200 doi
Amino Acid Motifs
Amino Acid Sequence
Eye Proteins--chemistry
Fluorescence Resonance Energy Transfer
Gelsolin--chemistry
Homeodomain Proteins--chemistry
Humans
Ligands
Molecular Sequence Data
Mutation
PAX6 Transcription Factor
Paired Box Transcription Factors--chemistry
Peptides--chemistry
Protein Binding
Protein Structure, Tertiary
Receptors, Androgen--chemistry
Repressor Proteins--chemistry
Sequence Homology, Amino Acid
Novel FXXFF and FXXMF motifs in androgen receptor cofactors mediate high affinity and specific interactions with the ligand-binding domain. [electronic resource] - The Journal of biological chemistry Jul 2006 - 19407-16 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.M602567200 doi
Amino Acid Motifs
Amino Acid Sequence
Eye Proteins--chemistry
Fluorescence Resonance Energy Transfer
Gelsolin--chemistry
Homeodomain Proteins--chemistry
Humans
Ligands
Molecular Sequence Data
Mutation
PAX6 Transcription Factor
Paired Box Transcription Factors--chemistry
Peptides--chemistry
Protein Binding
Protein Structure, Tertiary
Receptors, Androgen--chemistry
Repressor Proteins--chemistry
Sequence Homology, Amino Acid