CLONING OF THE AH-RECEPTOR CDNA REVEALS A DISTINCTIVE LIGAND-ACTIVATED TRANSCRIPTION FACTOR
CLONING OF THE AH-RECEPTOR CDNA REVEALS A DISTINCTIVE LIGAND-ACTIVATED TRANSCRIPTION FACTOR
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DOI：
10.1073/pnas.89.17.8185
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发表时间：
1992-09-01
影响因子：
11.1
通讯作者：
BRADFIELD, CA
中科院分区：
文献类型：
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作者：
BURBACH, KM;POLAND, A;BRADFIELD, CA
编码鼠Ah受体（芳烃反应性的Ah（B-1）等位基因）的cDNA已被分离和表征。推导的蛋白质序列的分析揭示了一个区域的相似性的基本区域/螺旋环螺旋（BR/HLH）基序中发现的许多转录因子进行二聚化的功能。除了BR/HLH结构域之外，Ah受体的N-末端结构域与人ARNT（芳烃受体核转运蛋白）蛋白和果蝇的两种调节蛋白Sim和Per具有广泛的序列相似性。光亲和标记和肽图谱的研究表明，Ah受体结合激动剂的结构域，位于这个保守的N-末端结构域。Ah受体似乎是一种配体激活的转录因子，其螺旋-环-螺旋基序类似于在多种DNA结合蛋白（包括Myc和MyoD）中发现的基序。
A cDNA encoding the murine Ah receptor (Ah(b-1) allele for aromatic hydrocarbon responsiveness) has been isolated and characterized. Analysis of the deduced protein sequence revealed a region with similarity to the basic region/helix-loop-helix (BR/HLH) motif found in many transcription factors that undergo dimerization for function. In addition to the BR/HLH domain, the N-terminal domain of the Ah receptor has extensive sequence similarity to the human ARNT (aryl hydrocarbon receptor nuclear translocator) protein and two regulatory proteins of Drosophila, Sim and Per. Photoaffinity labeling and peptide mapping studies indicate that the Ah receptor binds agonist at a domain that lies within this conserved N-terminal domain. The Ah receptor appears to be a ligand-activated transcription factor with a helix-loop-helix motif similar to those found in a variety of DNA-binding proteins, including Myc and MyoD.