Low-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution

The peroxisome proliferator-activated receptors (PPARs) regulate genes involved in lipid and carbohydrate metabolism, and are targets of drugs approved for human use. Whereas the crystallographic structure of the complex of full length PPARγ and RXRα is known, structural alterations induced by heter...

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Veröffentlicht in:	PloS one 2012-02, Vol.7 (2), p.e31852-e31852
Hauptverfasser:	Bernardes, Amanda, Batista, Fernanda A H, de Oliveira Neto, Mario, Figueira, Ana Carolina M, Webb, Paul, Saidemberg, Daniel, Palma, Mario S, Polikarpov, Igor
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding sites Biochemistry Biology Carbohydrate metabolism Carbohydrates Chromatography, Gel Conformation Contact angle Crystal structure Crystallography Deoxyribonucleic acid Deuterium Deuterium Exchange Measurement Diabetes Dimers DNA DNA - metabolism Drug approval Humans Hydrodynamics Hydrogen Immunology Ligands Lipid metabolism Mass Spectrometry Medicine Metabolism Models, Molecular Molecular modelling Molecular Sequence Data Molecular structure Nuclear receptors Peroxisome proliferator-activated receptors Physics Physiological aspects PPAR gamma - chemistry PPAR gamma - metabolism Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Proteins Receptors Response Elements - genetics Retinoid X Receptor alpha - chemistry Retinoid X Receptor alpha - metabolism Retinoid X receptors Scattering, Small Angle Scientific imaging Small angle X ray scattering Solutions X ray scattering X rays X-Ray Diffraction
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