RA Mediated T-reg Differentiation: Difference between revisions
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<StructureSection load='1dkf' size='350' side='left' caption='RARα-RXRα interaction (PDB entry [[1dkf]])' scene=''> | <StructureSection load='1dkf' size='350' side='left' caption='RARα-RXRα interaction (PDB entry [[1dkf]])' scene=''> | ||
==Ligand Binding Domain== | ==Ligand Binding Domain== | ||
The Ligand binding domain for each piece of the dimer has a nearly identical structure of an <scene name='RA_Mediated_T-reg_Differentiaition/Alpha-helical_domains/2'>Tα-helical sandwich</scene>. These alpha helices form a total of 12 domains per protein (referred to as H1-12), with an additional 2 beta sheets as well. Both monomers contain two regions of activity, the <scene name='RA_Mediated_T-reg_Differentiaition/Dimerization_interface/3'>dimerization interface</scene> and the ligand binding | The Ligand binding domain for each piece of the dimer has a nearly identical structure of an <scene name='RA_Mediated_T-reg_Differentiaition/Alpha-helical_domains/2'>Tα-helical sandwich</scene>. These alpha helices form a total of 12 domains per protein (referred to as H1-12), with an additional 2 beta sheets as well. Additionally, the α-helical sandwich formed has been shown to bind All-Trans Retinoic Acid, the isomer of RA used by the body. Both monomers contain two regions of activity, the <scene name='RA_Mediated_T-reg_Differentiaition/Dimerization_interface/3'>dimerization interface</scene> and the <scene name='RA_Mediated_T-reg_Differentiaition/Ligand_binding_pockets/1'> ligand binding pocket </scene> .<ref> PMID: 10882070 </ref> | ||