视黄酸受体α配体结合域上光亲和标记位点的确定。
Determination of the photoaffinity-labeled site on the ligand-binding domain of retinoic acid receptor alpha.
作者信息
Sasaki T, Shimazawa R, Sawada T, Iijima T, Fukasawa H, Shudo K, Hashimoto Y, Iwasaki S
机构信息
Institute of Molecular and Cellular Biosciences, University of Tokyo, Japan.
出版信息
Biochem Biophys Res Commun. 1995 Feb 6;207(1):444-51. doi: 10.1006/bbrc.1995.1208.
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.
通过使用由麦芽糖结合蛋白和人视黄酸受体α（hRARα）的E/F结构域构建的重组融合蛋白（MBP-RARα/E），该融合蛋白在大肠杆菌中表达，人视黄酸受体α（hRARα）的配体结合结构域用荧光类视黄醇ADAM-3进行了光亲和标记。标记位点被确定为Arg-589（这对应于hRARα的氨基酸残基385）或其附近的一个残基。
Zotero 插件