Determination of the photoaffinity-labeled site on the ligand-binding domain of retinoic acid receptor alpha.
The ligand-binding domain of human retinoic acid receptor alpha (hRAR alpha) was photoaffinity-labeled with a fluorescent retinoid, ADAM-3, by the use of a recombinant fused protein constructed from a maltose-binding protein and the E/F-domain of hRAR alpha (MBP-RAR alpha/E), which was expressed in E. coli. The labeled site was identified as Arg-589 (this corresponds to amino acid residue 385 of hRAR alpha) or a residue in its vicinity.
Sasaki
T
T
Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.
Shimazawa
R
R
Sawada
T
T
Iijima
T
T
Fukasawa
H
H
Shudo
K
K
Hashimoto
Y
Y
Iwasaki
S
S
D000345:Affinity Labels; D000595:Amino Acid Sequence; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases; D004926:Escherichia coli; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D018168:Receptors, Retinoic Acid / Q000737:chemistry / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D000072482:Retinoic Acid Receptor alpha; D012176:Retinoids / Q000737:chemistry* / Q000378:metabolism
C091976:ADAM 3; D000345:Affinity Labels; D008024:Ligands; D010446:Peptide Fragments; C000607071:RARA protein, human; D018168:Receptors, Retinoic Acid; D011993:Recombinant Fusion Proteins; D000072482:Retinoic Acid Receptor alpha; D012176:Retinoids; D010450:Endopeptidases