PPAR-gamma - Revision history

Michal Harel at 09:33, 12 January 2023

Michal Harel — Thu, 12 Jan 2023 09:33:23 GMT

←Older revision		Revision as of 09:33, 12 January 2023
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-	<StructureSection load='3et3' size='450' side='right' scene='' caption='Human PPAR-gamma (grey) complex with NCOA-1 peptide (green) (PDB code [[3et3]]) '>	+	<StructureSection load='3et3' size='450' side='right' scene='' caption='Human PPAR-gamma (grey) complex with NCOA-1 peptide (green) and anti-diabetic agent (PDB code [[3et3]]) '>

	== Introduction ==		== Introduction ==

Michal Harel at 09:31, 12 January 2023

Michal Harel — Thu, 12 Jan 2023 09:31:56 GMT

←Older revision		Revision as of 09:31, 12 January 2023
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-	<StructureSection load='3et3' size='450' side='right' scene='' caption=''>	+	<StructureSection load='3et3' size='450' side='right' scene='' caption='Human PPAR-gamma (grey) complex with NCOA-1 peptide (green) (PDB code [[3et3]]) '>

	== Introduction ==		== 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.		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.
		+
		+	See also [[Intracellular receptors]]

	== Overall Structure and Ligand Binding ==		== Overall Structure and Ligand Binding ==

Alexander Berchansky at 12:20, 1 August 2013

Alexander Berchansky — Thu, 01 Aug 2013 12:20:27 GMT

←Older revision		Revision as of 12:20, 1 August 2013
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-	<~~applet~~ load='3et3' size='~~400~~' ~~frame~~='~~true~~' ~~align~~='~~right~~' caption='~~PPAR gamma complex with steroid receptor coactivator peptide and anti-diabetic agent [[3et3]]' name='1~~' />	+	<StructureSection load='3et3' size='450' side='right' scene='' caption=''>

	== Introduction ==		== Introduction ==
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	PPARγ is composed of the ligand-independent activation domain (AF-1 region and A/B-domain), a DNA-binding domain (DBD) (C-domain), a hinge region (D-domain), and a ligand-dependent ligand-binding domain (LBD) (E/F-domain and AF-2 region) [5]. The two PPARγ isoforms, PPARγ1 and PPARγ2, differ by only 30 amino acids at the N-terminal end. These added amino acids on PPARγ2 result in increased potency and adipose-selectivity, which makes this protein a key player of adipocyte differentiation [3].		PPARγ is composed of the ligand-independent activation domain (AF-1 region and A/B-domain), a DNA-binding domain (DBD) (C-domain), a hinge region (D-domain), and a ligand-dependent ligand-binding domain (LBD) (E/F-domain and AF-2 region) [5]. The two PPARγ isoforms, PPARγ1 and PPARγ2, differ by only 30 amino acids at the N-terminal end. These added amino acids on PPARγ2 result in increased potency and adipose-selectivity, which makes this protein a key player of adipocyte differentiation [3].
	The <scene name='PPAR-gamma/Lbd/2' target='2'>ligand binding domain</scene> is composed of 13 α helices and 4 short β strands [1]. It has a T-shaped binding pocket with a volume of ~1440 Å3 [1, 6], which is larger than that of most nuclear receptors [7], allowing for interactions with a variety of ligands [8]. The PPARγ LBD is folded into a helical sandwich to provide a binding site for ligands. It is located at the C-terminal end of PPARγ and is composed of about 250 amino acids [5]. Activation by full agonists occurs through hydrogen bond interactions between the S289, H323, Y473, and H449 residues of the PPARγ-LBD [7] and polar functional groups on the ligand which are typically carbonyl or carboxyl oxygen atoms. Agonist binding results in a conformational change of the LBD AF-2 region, which is necessary for coactivator recruitment. This change can either be dramatic or subtle [1], which leads to stabilization of a charge clamp between helices H3 and H12 [9] to aid in associations with the LXXLL (L, leucine; X, any amino acid) motif of the coactivator [1, 10]. Ligand binding of PPARγ is regulated by communication between the N-terminal A/B domain, which is adjacent to the DBD, and the carboxyl-terminal LBD [11].		The <scene name='PPAR-gamma/Lbd/2' target='2'>ligand binding domain</scene> is composed of 13 α helices and 4 short β strands [1]. It has a T-shaped binding pocket with a volume of ~1440 Å3 [1, 6], which is larger than that of most nuclear receptors [7], allowing for interactions with a variety of ligands [8]. The PPARγ LBD is folded into a helical sandwich to provide a binding site for ligands. It is located at the C-terminal end of PPARγ and is composed of about 250 amino acids [5]. Activation by full agonists occurs through hydrogen bond interactions between the S289, H323, Y473, and H449 residues of the PPARγ-LBD [7] and polar functional groups on the ligand which are typically carbonyl or carboxyl oxygen atoms. Agonist binding results in a conformational change of the LBD AF-2 region, which is necessary for coactivator recruitment. This change can either be dramatic or subtle [1], which leads to stabilization of a charge clamp between helices H3 and H12 [9] to aid in associations with the LXXLL (L, leucine; X, any amino acid) motif of the coactivator [1, 10]. Ligand binding of PPARγ is regulated by communication between the N-terminal A/B domain, which is adjacent to the DBD, and the carboxyl-terminal LBD [11].
-
-	<applet load='2f4b' size='300' frame='true' align='left' caption='PPARγ Ligand Binding Domain complex with agonist [[2f4b]]' name='2' />

	== Ligand Activity ==		== Ligand Activity ==
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	PPARγ is found in high levels in colonic epithelial cells. The role of PPARγ in these cells may be related to regulation of immune response and colon inflammation [12]. The onset of Inflammatory Bowel Disease is thought to be caused by inflammatory cytokines present in the colon [12]. In patients with ulcerative colitis, colonic epithelial cells displayed impaired expression of PPARγ, an important mediator of aminosalicylate activities in Inflammatory Bowel Diseases [13]. TZD ligands could be implemented to reduce colonic inflammation [12]. Agonists have also been used in the treatment of colitis and psoriasis by inhibiting the inflammatory response of the epithelium and reducing cytokine production [8]. PPARγ inhibits activity of nuclear factor NFκB, which is higher in active ulcerative colitis patients [15].		PPARγ is found in high levels in colonic epithelial cells. The role of PPARγ in these cells may be related to regulation of immune response and colon inflammation [12]. The onset of Inflammatory Bowel Disease is thought to be caused by inflammatory cytokines present in the colon [12]. In patients with ulcerative colitis, colonic epithelial cells displayed impaired expression of PPARγ, an important mediator of aminosalicylate activities in Inflammatory Bowel Diseases [13]. TZD ligands could be implemented to reduce colonic inflammation [12]. Agonists have also been used in the treatment of colitis and psoriasis by inhibiting the inflammatory response of the epithelium and reducing cytokine production [8]. PPARγ inhibits activity of nuclear factor NFκB, which is higher in active ulcerative colitis patients [15].
	PPARγ could also be implemented in the treatment of other chronic inflammation-related diseases. Immunomodulatory effects have been found with PPARγ agonists [16]. Rosiglitazone alongside adiponectin reduces renal disease, atherosclerosis, and production of autoantibodies, all of which are characteristic of the inflammatory autoimmune disease Systemic Lupus Erythematosus (SLE) [16]. PPARγ ligands hold potential as cancer treatments [11] due to their ability to inhibit angiogenesis, the process required for the growth and metastasis of solid tumors [8]. PPARγ activators have pro-differentiation and anti-proliferation effects [3]. TZDs have also been shown to inhibit proliferation of human breast, prostate, and colon cancer cells [8].		PPARγ could also be implemented in the treatment of other chronic inflammation-related diseases. Immunomodulatory effects have been found with PPARγ agonists [16]. Rosiglitazone alongside adiponectin reduces renal disease, atherosclerosis, and production of autoantibodies, all of which are characteristic of the inflammatory autoimmune disease Systemic Lupus Erythematosus (SLE) [16]. PPARγ ligands hold potential as cancer treatments [11] due to their ability to inhibit angiogenesis, the process required for the growth and metastasis of solid tumors [8]. PPARγ activators have pro-differentiation and anti-proliferation effects [3]. TZDs have also been shown to inhibit proliferation of human breast, prostate, and colon cancer cells [8].
-		+	</StructureSection>
		+	__NOTOC__
	==3D structures of PPAR==		==3D structures of PPAR==

Michal Harel at 11:40, 31 January 2012

Michal Harel — Tue, 31 Jan 2012 11:40:08 GMT

←Older revision		Revision as of 11:40, 31 January 2012
Line 33:		Line 33:
	PPARγ is found in high levels in colonic epithelial cells. The role of PPARγ in these cells may be related to regulation of immune response and colon inflammation [12]. The onset of Inflammatory Bowel Disease is thought to be caused by inflammatory cytokines present in the colon [12]. In patients with ulcerative colitis, colonic epithelial cells displayed impaired expression of PPARγ, an important mediator of aminosalicylate activities in Inflammatory Bowel Diseases [13]. TZD ligands could be implemented to reduce colonic inflammation [12]. Agonists have also been used in the treatment of colitis and psoriasis by inhibiting the inflammatory response of the epithelium and reducing cytokine production [8]. PPARγ inhibits activity of nuclear factor NFκB, which is higher in active ulcerative colitis patients [15].		PPARγ is found in high levels in colonic epithelial cells. The role of PPARγ in these cells may be related to regulation of immune response and colon inflammation [12]. The onset of Inflammatory Bowel Disease is thought to be caused by inflammatory cytokines present in the colon [12]. In patients with ulcerative colitis, colonic epithelial cells displayed impaired expression of PPARγ, an important mediator of aminosalicylate activities in Inflammatory Bowel Diseases [13]. TZD ligands could be implemented to reduce colonic inflammation [12]. Agonists have also been used in the treatment of colitis and psoriasis by inhibiting the inflammatory response of the epithelium and reducing cytokine production [8]. PPARγ inhibits activity of nuclear factor NFκB, which is higher in active ulcerative colitis patients [15].
	PPARγ could also be implemented in the treatment of other chronic inflammation-related diseases. Immunomodulatory effects have been found with PPARγ agonists [16]. Rosiglitazone alongside adiponectin reduces renal disease, atherosclerosis, and production of autoantibodies, all of which are characteristic of the inflammatory autoimmune disease Systemic Lupus Erythematosus (SLE) [16]. PPARγ ligands hold potential as cancer treatments [11] due to their ability to inhibit angiogenesis, the process required for the growth and metastasis of solid tumors [8]. PPARγ activators have pro-differentiation and anti-proliferation effects [3]. TZDs have also been shown to inhibit proliferation of human breast, prostate, and colon cancer cells [8].		PPARγ could also be implemented in the treatment of other chronic inflammation-related diseases. Immunomodulatory effects have been found with PPARγ agonists [16]. Rosiglitazone alongside adiponectin reduces renal disease, atherosclerosis, and production of autoantibodies, all of which are characteristic of the inflammatory autoimmune disease Systemic Lupus Erythematosus (SLE) [16]. PPARγ ligands hold potential as cancer treatments [11] due to their ability to inhibit angiogenesis, the process required for the growth and metastasis of solid tumors [8]. PPARγ activators have pro-differentiation and anti-proliferation effects [3]. TZDs have also been shown to inhibit proliferation of human breast, prostate, and colon cancer cells [8].
		+
		+	==3D structures of PPAR==
		+
		+	[[Peroxisome Proliferator-Activated Receptors]]

	==Additional Resources==		==Additional Resources==

Michal Harel at 08:40, 14 August 2011

Michal Harel — Sun, 14 Aug 2011 08:40:40 GMT

←Older revision		Revision as of 08:40, 14 August 2011
Line 10:		Line 10:
	The <scene name='PPAR-gamma/Lbd/2' target='2'>ligand binding domain</scene> is composed of 13 α helices and 4 short β strands [1]. It has a T-shaped binding pocket with a volume of ~1440 Å3 [1, 6], which is larger than that of most nuclear receptors [7], allowing for interactions with a variety of ligands [8]. The PPARγ LBD is folded into a helical sandwich to provide a binding site for ligands. It is located at the C-terminal end of PPARγ and is composed of about 250 amino acids [5]. Activation by full agonists occurs through hydrogen bond interactions between the S289, H323, Y473, and H449 residues of the PPARγ-LBD [7] and polar functional groups on the ligand which are typically carbonyl or carboxyl oxygen atoms. Agonist binding results in a conformational change of the LBD AF-2 region, which is necessary for coactivator recruitment. This change can either be dramatic or subtle [1], which leads to stabilization of a charge clamp between helices H3 and H12 [9] to aid in associations with the LXXLL (L, leucine; X, any amino acid) motif of the coactivator [1, 10]. Ligand binding of PPARγ is regulated by communication between the N-terminal A/B domain, which is adjacent to the DBD, and the carboxyl-terminal LBD [11].		The <scene name='PPAR-gamma/Lbd/2' target='2'>ligand binding domain</scene> is composed of 13 α helices and 4 short β strands [1]. It has a T-shaped binding pocket with a volume of ~1440 Å3 [1, 6], which is larger than that of most nuclear receptors [7], allowing for interactions with a variety of ligands [8]. The PPARγ LBD is folded into a helical sandwich to provide a binding site for ligands. It is located at the C-terminal end of PPARγ and is composed of about 250 amino acids [5]. Activation by full agonists occurs through hydrogen bond interactions between the S289, H323, Y473, and H449 residues of the PPARγ-LBD [7] and polar functional groups on the ligand which are typically carbonyl or carboxyl oxygen atoms. Agonist binding results in a conformational change of the LBD AF-2 region, which is necessary for coactivator recruitment. This change can either be dramatic or subtle [1], which leads to stabilization of a charge clamp between helices H3 and H12 [9] to aid in associations with the LXXLL (L, leucine; X, any amino acid) motif of the coactivator [1, 10]. Ligand binding of PPARγ is regulated by communication between the N-terminal A/B domain, which is adjacent to the DBD, and the carboxyl-terminal LBD [11].

-	<applet load='2f4b' size='300' frame='true' align='left' caption='PPARγ Ligand Binding Domain' name='2' />	+	<applet load='2f4b' size='300' frame='true' align='left' caption='PPARγ Ligand Binding Domain complex with agonist [[2f4b]]' name='2' />

	== Ligand Activity ==		== Ligand Activity ==

Michal Harel at 08:38, 14 August 2011

Michal Harel — Sun, 14 Aug 2011 08:38:26 GMT

←Older revision		Revision as of 08:38, 14 August 2011
Line 1:		Line 1:
-	<applet load='3et3' size='400' frame='true' align='right' caption='PPAR gamma [[3et3]]' name='1' />	+	<applet load='3et3' size='400' frame='true' align='right' caption='PPAR gamma complex with steroid receptor coactivator peptide and anti-diabetic agent [[3et3]]' name='1' />

	== Introduction ==		== Introduction ==

Michal Harel at 08:31, 14 August 2011

Michal Harel — Sun, 14 Aug 2011 08:31:44 GMT

←Older revision		Revision as of 08:31, 14 August 2011
Line 1:		Line 1:
-	<applet load='3et3' size='400' frame='true' align='right' caption='PPAR gamma' name='1' />	+	<applet load='3et3' size='400' frame='true' align='right' caption='PPAR gamma [[3et3]]' name='1' />

	== Introduction ==		== Introduction ==

David Canner at 13:16, 3 October 2010

David Canner — Sun, 03 Oct 2010 13:16:06 GMT

←Older revision		Revision as of 13:16, 3 October 2010
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	==Additional Resources==		==Additional Resources==
-	For additional information See: [[Diabetes]]	+	For additional information See: [[Diabetes]]<br/>
-	For additional information See: [[Regulation of Gene Expression]]	+	For additional information See: [[Regulation of Gene Expression]] <br/>
	For additional information See: [[Peroxisome Proliferator-Activated Receptors]]		For additional information See: [[Peroxisome Proliferator-Activated Receptors]]
	<br/>		<br/>

David Canner at 13:15, 3 October 2010

David Canner — Sun, 03 Oct 2010 13:15:46 GMT

←Older revision		Revision as of 13:15, 3 October 2010
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	== PPARγ/RXRα ==		== PPARγ/RXRα ==

-	PPARγ shows preferential heterodimerization with RXRα [3]. The asymmetry of PPARγ/RXRα packs positively and negatively charged regions together, and is needed for PPARγ binding to DNA [1]. The LBD and DBD of PPARγ are located close together, whereas the RXRα LBD and DBD are positioned farther apart. This difference in region proximity plays a role in heterodimerization [5]. The PPARγ/RXRα complex associates with PPAR response elements (PPREs) in promoter regions of targeted genes [8]. Each ligand-bound PPAR/RXRα complex will bind to a specific PPRE based on the recruited cofactor [8].	+	PPARγ shows preferential heterodimerization with RXRα [3]. The asymmetry of PPARγ/RXRα packs positively and negatively charged regions together, and is needed for PPARγ binding to [[DNA]] [1]. The LBD and DBD of PPARγ are located close together, whereas the RXRα LBD and DBD are positioned farther apart. This difference in region proximity plays a role in heterodimerization [5]. The PPARγ/RXRα complex associates with PPAR response elements (PPREs) in promoter regions of targeted genes [8]. Each ligand-bound PPAR/RXRα complex will bind to a specific PPRE based on the recruited cofactor [8].

	== Functions ==		== Functions ==
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	==Additional Resources==		==Additional Resources==
-	For additional information See: [[Regulation of Gene Expression]] or [[Peroxisome Proliferator-Activated Receptors]]	+	For additional information See: [[Diabetes]]
		+	For additional information See: [[Regulation of Gene Expression]]
		+	For additional information See: [[Peroxisome Proliferator-Activated Receptors]]
	<br/>		<br/>

David Canner at 13:13, 3 October 2010

David Canner — Sun, 03 Oct 2010 13:13:18 GMT

←Older revision		Revision as of 13:13, 3 October 2010
Line 3:		Line 3:
	== Introduction ==		== 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.	+	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 ==		== Overall Structure and Ligand Binding ==
Line 35:		Line 35:

	==Additional Resources==		==Additional Resources==
-	For additional information See: [[Regulation of Gene Expression]]	+	For additional information See: [[Regulation of Gene Expression]] or [[Peroxisome Proliferator-Activated Receptors]]
	<br/>		<br/>