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1prg
From Proteopedia
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| - | [[Image:1prg.gif|left|200px]]<br /><applet load="1prg" size=" | + | [[Image:1prg.gif|left|200px]]<br /><applet load="1prg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1prg, resolution 2.20Å" /> | caption="1prg, resolution 2.20Å" /> | ||
'''LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA'''<br /> | '''LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Known structural/functional Sites: <scene name='pdbsite=LLL:These Residues Are Involved In Binding The Lxxll Helix O ...'>LLL</scene> and <scene name='pdbsite=LND:These Residues Are Involved In Ligand Binding'>LND</scene>. Full crystallographic information is available from [http:// | + | 1PRG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Known structural/functional Sites: <scene name='pdbsite=LLL:These+Residues+Are+Involved+In+Binding+The+Lxxll+Helix+O+...'>LLL</scene> and <scene name='pdbsite=LND:These+Residues+Are+Involved+In+Ligand+Binding'>LND</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:00:01 2008'' |
Revision as of 08:00, 3 February 2008
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LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA
Contents |
Overview
The peroxisome proliferator-activated receptor-gamma (PPAR-gamma) is a, ligand-dependent transcription factor that is important in adipocyte, differentiation and glucose homeostasis and which depends on interactions, with co-activators, including steroid receptor co-activating factor-1, (SRC-1). Here we present the X-ray crystal structure of the human, apo-PPAR-gamma ligand-binding domain (LBD), at 2.2 A resolution; this, structure reveals a large binding pocket, which may explain the diversity, of ligands for PPAR-gamma. We also describe the ternary complex containing, the PPAR-gamma LBD, the antidiabetic ligand rosiglitazone (BRL49653), and, 88 amino acids of human SRC-1 at 2.3 A resolution. Glutamate and lysine, residues that are highly conserved in LBDs of nuclear receptors form a, 'charge clamp' that contacts backbone atoms of the LXXLL helices of SRC-1., These results, together with the observation that two consecutive LXXLL, motifs of SRC-1 make identical contacts with both subunits of a PPAR-gamma, homodimer, suggest a general mechanism for the assembly of nuclear, receptors with co-activators.
Disease
Known diseases associated with this structure: Abdominal body fat distribution, modifier of OMIM:[601487], Diabetes mellitus, insulin-resistant, with acanthosis nigricans and hypertension OMIM:[601487], Glioblastoma, susceptibility to OMIM:[601487], Insulin resistance, severe, digenic OMIM:[601487], Lipodystrophy, familial partial OMIM:[601487], Obesity, resistance to OMIM:[601487], Obesity, severe OMIM:[601487]
About this Structure
1PRG is a Single protein structure of sequence from Homo sapiens. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma., Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV, Nature. 1998 Sep 10;395(6698):137-43. PMID:9744270
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