Sandbox Reserved 490: Difference between revisions
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{{Sandbox_Reserved_Robert_B_Rose_1}} | {{Sandbox_Reserved_Robert_B_Rose_1}} | ||
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
== '''Estrogen Receptor''' == | == '''Estrogen Receptor''' == | ||
== Introduction == | == Introduction == | ||
Estrogen receptors (ER) belong to the super family of nuclear receptor proteins (NRP). Nuclear receptor proteins are a diverse group of proteins located in the nucleus. These proteins bind to specific ligands and undergo conformational changes, whereby they can then act as transcription factors to up-regulate or down-regulate certain genes. Nuclear hormone receptors (NHR) are a subgroup of NRPs that have hormone ligands. Estrogen receptors are nuclear hormone receptors whose ligand is estrogen.[http://www.jbc.org/content/276/40/36863] NRPs are found only in animals.[http://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.1998.tb10747.x/pdf] | Estrogen receptors (ER) belong to the super family of nuclear receptor proteins (NRP). Nuclear receptor proteins are a diverse group of proteins located in the nucleus. These proteins bind to specific ligands and undergo conformational changes, whereby they can then act as transcription factors to up-regulate or down-regulate certain genes. Nuclear hormone receptors (NHR) are a subgroup of NRPs that have hormone ligands. Estrogen receptors are nuclear hormone receptors whose ligand is estrogen.[http://www.jbc.org/content/276/40/36863] NRPs are found only in animals.[http://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.1998.tb10747.x/pdf] | ||
There are two types of estrogen receptors: estrogen receptor-α and estrogen receptor-β. There has been much research done on both ERalpha and ERbeta, and it is still unclear exactly how each functions. However, like all NRPs, the ER proteins have a highly conserved DNA-binding domain, a specific ligand-binding domain, and a highly variable N-terminus region. In ER proteins, the ligand-binding domain is located near the C-terminal region of the protein. The ligand-binding domain of ERalpha and ERbeta are similar. Both ERalpha and ERbeta bind estrogen at the ligand-binding domain. Once bound, the mechanism of transcriptional regulation is dependent upon what co-factors and other signalling molecules are present in the cell.[http://physrev.physiology.org/content/87/3/905.full.pdf] | There are two types of estrogen receptors: estrogen receptor-α and estrogen receptor-β. There has been much research done on both ERalpha and ERbeta, and it is still unclear exactly how each functions. However, like all NRPs, the ER proteins have a highly conserved DNA-binding domain, a specific ligand-binding domain, and a highly variable N-terminus region. In ER proteins, the ligand-binding domain is located near the C-terminal region of the protein. The ligand-binding domain of ERalpha and ERbeta are similar. Both ERalpha and ERbeta bind estrogen at the ligand-binding domain. Once bound, the mechanism of transcriptional regulation is dependent upon what co-factors and other signalling molecules are present in the cell.[http://physrev.physiology.org/content/87/3/905.full.pdf] | ||
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== Structure == | == Structure == | ||
Estrogen receptors have two important structural components: the DNA-binding domain and the ligand-binding domain. | Estrogen receptors have two important structural components: the DNA-binding domain and the ligand-binding domain. | ||
''DNA-Binding domain'' | ''DNA-Binding domain'' | ||
<StructureSection load='1hcq' size='500' side='right' caption='Structure of Estrogen Receptor (PDB entry [[1hcq]])' scene=''>This is the structure of the estrogen receptor when its DNA binding domain is complexed to DNA. It binds as a <scene name='Sandbox_Reserved_490/Dbd_dimerization_domains/1'>symmetrical dimer</scene> to the appropriate DNA sequence. Each dimer consists of | |||
<StructureSection load='1hcq' size='500' side='right' caption='Structure of Estrogen Receptor (PDB entry [[1hcq]])' scene=''> | |||
This is the structure of the estrogen receptor when its DNA binding domain is complexed to DNA. It binds as a <scene name='Sandbox_Reserved_490/Dbd_dimerization_domains/1'>symmetrical dimer</scene> to the appropriate DNA sequence. Each dimer consists of | |||
<scene name='Sandbox_Reserved_490/Dbd_secondary_structure/1'>two alpha helices and two antiparallel beta-sheets</scene>. The <scene name='Sandbox_Reserved_490/Dbd_active_residues/1'>active residues</scene> are located on the <scene name='Sandbox_Reserved_490/Dbd_hydrophobic/1'>hydrophilic</scene> face of the <scene name='Sandbox_Reserved_490/Dbd_recognition_helix/1'>recognition helix</scene>. These residues follow a modified zinc finger motif. [http://www.sciencedirect.com/science/article/pii/009286749390390C] </StructureSection> | <scene name='Sandbox_Reserved_490/Dbd_secondary_structure/1'>two alpha helices and two antiparallel beta-sheets</scene>. The <scene name='Sandbox_Reserved_490/Dbd_active_residues/1'>active residues</scene> are located on the <scene name='Sandbox_Reserved_490/Dbd_hydrophobic/1'>hydrophilic</scene> face of the <scene name='Sandbox_Reserved_490/Dbd_recognition_helix/1'>recognition helix</scene>. These residues follow a modified zinc finger motif. [http://www.sciencedirect.com/science/article/pii/009286749390390C] </StructureSection> | ||
<Structure load='1HCQ' size='500' frame='true' align='right' caption='Estrogen Receptor DNA Binding Domain Complexed to DNA' scene='Insert optional scene name here' /> | <Structure load='1HCQ' size='500' frame='true' align='right' caption='Estrogen Receptor DNA Binding Domain Complexed to DNA' scene='Insert optional scene name here' /> | ||
