RA Mediated T-reg Differentiation: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

William Bailey, Michal Harel, Jaime Prilusky, Alexander Berchansky

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 <StructureSection load='1dkf' size='350' side='left' caption='RARα-RXRα interaction (PDB entry [[1dkf]])' scene=''>
 ==Ligand Binding Domain==
-The Ligand binding domain for each piece of the dimer has a very similar 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/2'>dimerization interface</scene> and the 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/2'>dimerization interface</scene> and the ligand binding domain.<ref> PMID: 10882070 </ref>
 === RARα-RXRα Heterodimer ===
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-The residues of RARα that are interacting in the heterodimer are as follows:
+The residues of <scene name='RA_Mediated_T-reg_Differentiaition/Rar_dimer_interface/1'> RAR-</scene>α that are interacting in the heterodimer are as follows:
 Hydrophobic residues: L356, F374, P375, L378, M379, I381 and A389 (yellow);
 Negatively charged residues: D338, D349, E353, E357, D383, and E393 (red);