Sandbox Reserved 490: Difference between revisions
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<Structure load='1a52' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='1a52' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
<StructureSection load='1a52' size='500' side='right' caption='Structure of Estrogen Receptor (PDB entry [[1a52]])' scene=''>The ligand-bound estrogen receptor is also a <scene name='Sandbox_Reserved_490/Lbd_dimers/1'>dimer</scene | <StructureSection load='1a52' size='500' side='right' caption='Structure of Estrogen Receptor (PDB entry [[1a52]])' scene=''>The ligand-bound estrogen receptor is also a <scene name='Sandbox_Reserved_490/Lbd_dimers/1'>dimer</scene>. Each unit has 12 <scene name='Sandbox_Reserved_490/Lbd_secondary_structure/1'>alpha helices and one antiparallel beta sheet</scene>. The <scene name='Sandbox_Reserved_490/Lbd_hydropobic_polar/1'>hydrophobic</scene> faces of the helices participating in the dimerization process face each other. | ||
The ligand-binding domain of each unit involves <scene name='Sandbox_Reserved_490/Lbd_active_residues/1'>key residues</scene> from helices 7, 8, and 9 in the binding pocket. Most of the residues are hydrophobic, to interact with the hydrophobic portions of the estrogen steroid. The Glu-353 and His-524 hydrogen bond directly with the hydroxyl groups on the estrogen ligand.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC27574/] | The ligand-binding domain of each unit involves <scene name='Sandbox_Reserved_490/Lbd_active_residues/1'>key residues</scene> from helices 7, 8, and 9 in the binding pocket. Most of the residues are hydrophobic, to interact with the hydrophobic portions of the estrogen steroid. The Glu-353 and His-524 hydrogen bond directly with the hydroxyl groups on the estrogen ligand.[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC27574/] | ||