Peroxisome Proliferator-Activated Receptors: Difference between revisions

David Canner (talk | contribs)
No edit summary
David Canner (talk | contribs)
No edit summary
Line 48: Line 48:
===DNA Binding Domain Structure===
===DNA Binding Domain Structure===
[[Image:Rosiglitazone.png|300px|left|thumb| Human PPARγ agonist, Rosiglitazone (Avandia)]]
[[Image:Rosiglitazone.png|300px|left|thumb| Human PPARγ agonist, Rosiglitazone (Avandia)]]
PPARs also contain a DNA binding domain (DBD) The <scene name='Peroxisome_Proliferator-Activated_Receptors/Zinc_fingers/1'>DBD consist of two zinc fingers</scene>, one on PPAR and one on RXR, that bind PPREs of PPAR-responsive genes. The consensus sequence of PPREs is AGGTCA and has been found in a number of PPAR inducible genes like acyl-CoA oxidase and adipocyte fatty acid-binding protein.<ref>PMID:9383428</ref> It is believed that the DNA PPRE actually allosterically contributes to its own binding by directing a head-to-tail interaction between the PPAR DBD and RXR DBD via residues Gln206 and Arg209 on RXRα and Asn160 on PPARγ.<ref>PMID:19043829</ref>
PPARs also contain a DNA binding domain (DBD) The <scene name='Peroxisome_Proliferator-Activated_Receptors/Zinc_fingers/1'>DBD consist of two zinc fingers</scene>, one on PPAR and one on RXR, that bind PPREs of PPAR-responsive genes. The consensus sequence of PPREs is AGGTCA and has been found in a number of PPAR inducible genes like acyl-CoA oxidase and adipocyte fatty acid-binding protein.<ref>PMID:9383428</ref> It is believed that the DNA PPRE actually allosterically contributes to its own binding by via a <scene name='Peroxisome_Proliferator-Activated_Receptors/Dbd_hbonds/1'>head-to-tail interaction between the PPAR DBD and RXR DBD</scene> using residues Gln206 and Arg209 on RXRα and Asn160 on PPARγ.<ref>PMID:19043829</ref>
<br />
<br />
==Binding of Synthetic Agonists and Medical Implications==
==Binding of Synthetic Agonists and Medical Implications==

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

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