Nuclear receptors are a class of proteins that are found within the cell nucleus and play a key role in regulating gene expression. These receptors are typically composed of several structural domains that are important for their function. The main structural components of nuclear receptors include:
1. DNA-binding domain (DBD): This domain is responsible for binding to specific DNA sequences known as hormone response elements (HREs) within the promoter regions of target genes. The DBD contains a zinc finger motif that allows the receptor to recognize and bind to its target DNA sequences.
2. Ligand-binding domain (LBD): This domain is responsible for binding to specific ligands, such as hormones or other signaling molecules, that activate the receptor. The LBD contains a ligand-binding pocket that can accommodate the ligand molecule and induce conformational changes in the receptor that allow it to interact with coactivator proteins and regulate gene expression.
3. Activation function domains (AF-1 and AF-2): These domains are located within the N-terminal and C-terminal regions of the receptor, respectively, and are important for recruiting coactivator proteins that are necessary for activating gene transcription. The AF-1 domain is typically involved in ligand-independent activation of the receptor, while the AF-2 domain is activated upon ligand binding.
4. Nuclear localization signal (NLS): This signal sequence is responsible for directing the receptor to the nucleus, where it can interact with DNA and regulate gene expression.
Overall, the structure of nuclear receptors allows them to function as ligand-activated transcription factors that regulate the expression of target genes in response to specific signaling molecules.
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Google Gemini AI
3 hours ago
Nuclear receptors (NRs) are a large family of transcription factors that regulate gene expression in response to a variety of stimuli, including hormones, vitamins, and xenobiotics. NRs are modular proteins that contain several distinct domains, each with a specific function.
The structure of NRs is as follows:
- N-terminal domain (NTD): The NTD is responsible for ligand binding. It contains a ligand-binding pocket that is specific for a particular ligand. - DNA-binding domain (DBD): The DBD is responsible for binding to DNA. It contains a zinc finger motif that recognizes specific DNA sequences. - Hinge region: The hinge region is a flexible linker that connects the NTD and DBD. It allows the NTD and DBD to move independently of each other. - Ligand-dependent activation function (AF-2): The AF-2 is a domain that is responsible for activating transcription. It is located in the C-terminal region of the NR. - Ligand-independent activation function (AF-1): The AF-1 is a domain that is responsible for activating transcription in the absence of ligand. It is located in the N-terminal region of the NR.
The structure of NRs is highly conserved. This conservation is likely due to the fact that NRs play a critical role in a variety of cellular processes, including metabolism, development, and reproduction. Mutations in NR genes have been linked to a number of diseases, including cancer, diabetes, and obesity.