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pubmed-article:7857302pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:7857302pubmed:articleTitleDetermination of the photoaffinity-labeled site on the ligand-binding domain of retinoic acid receptor alpha.lld:pubmed
pubmed-article:7857302pubmed:affiliationInstitute of Molecular and Cellular Biosciences, University of Tokyo, Japan.lld:pubmed
pubmed-article:7857302pubmed:publicationTypeJournal Articlelld:pubmed