Peroxisome Proliferator-Activated Receptors: Difference between revisions

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David Canner, Alexander Berchansky, Michal Harel, Joel L. Sussman

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 ===AF-2 Domain: Structure and Function===
 <applet load="2prg2.pdb" size="450" color="white" frame="true" spin="on" Scene ="Peroxisome_Proliferator-Activated_Receptors/Ppar_opening3/2" caption="Crystal Structure of Human PPAR" align="right"/>
-As briefly mentioned before, the AF-2 domain is essential for ligand binding and <scene name='Peroxisome_Proliferator-Activated_Receptors/Ppar_opening3/2'>PPAR</scene> function. Upon ligand binding, helix H12 of AF-2 closes on the ligand-binding site, reducing conformational flexibility of the LBD and assuming a structure that is ideal for co-activator binding. Using Molecular Dynamic simulations, it has been determined that residues <scene name='Peroxisome_Proliferator-Activated_Receptors/H_bonding_network/3'>Glu324, Arg397, Arg443, and Tyr 477</scene> (in PPARγ) are involved in a hydrogen bond network that stabilizes the AF-2 helix in the active conformation upon ligand binding.<ref>PMID:7501014</ref>
+As briefly mentioned before, the AF-2 domain is essential for ligand binding and <scene name='Peroxisome_Proliferator-Activated_Receptors/Ppar_opening3/2'>PPAR</scene> function. Upon ligand binding, helix H12 of AF-2 closes on the ligand-binding site, reducing conformational flexibility of the LBD and assuming a structure that is ideal for co-activator binding. Using Molecular Dynamic simulations, it has been determined that residues <scene name='Peroxisome_Proliferator-Activated_Receptors/H_bonding_network/3'>Glu324, Arg397, Arg443, and Tyr 477</scene> (in PPARγ) are involved in a hydrogen bond network that stabilizes the AF-2 helix in the active conformation upon ligand binding.<ref name="Zoete"/>
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