PPAR-gamma: Difference between revisions

== Introduction ==  

Peroxisome proliferator-activated receptor gamma (<scene name='PPAR-gamma/Ppar_gamma/3'>PPAR</scene>γ) is a protein in the nuclear receptors subfamily.  It is one of three isotypes (-α, -β/ δ, and -γ) [1] of [[PPAR]] receptors and has two protein isoforms governed by splice variations, which result in differences in the length of the amino (N)-terminal region (PPARγ1 and PPARγ2) [2].  PPARγ is involved in transcriptional regulation of glucose and lipid homeostasis [1], and helps regulate adipocyte differentiation [3].  It has a <scene name='PPAR-gamma/Binding_pocket/1' target='1'>large binding pocket</scene>, which allows it to interact with a wide array of ligands.  <scene name='PPAR-gamma/Interacting_residues/3'>Ligand binding</scene> typically triggers a conformational change of PPARγ, notably in the activation function-2 <scene name='PPAR-gamma/Af-2_domain/2'>(AF-2) domain</scene>, which aids in the recruitment of co-regulatory factors to regulate gene transcription.  PPARγ can form a <scene name='PPAR-gamma/Ppar_rxr/3'>heterodimer</scene> with retinoic X receptor alpha (RXRα), a process necessary for most PPARγ-DNA interactions [4].  PPARγ is a molecular target for antidiabetic drugs such as thiazolidinediones (TZDs), which makes the protein a target for Type II Diabetes (T2D) drug research.  Due to its involvement in metabolic and inflammatory processes, PPARγ also holds potential for treatments of many metabolic and chronic-inflammatory diseases, such as metabolic syndrome and inflammatory bowel disease, respectively.  Errors in PPARγ-related regulation have also been implicated in atherosclerosis and various cancers, like colorectal, breast, and prostate cancers.

== Overall Structure and Ligand Binding ==