Dynamic correlation networks in human peroxisome proliferator-activated receptor-γ nuclear receptor protein
Impacto
Scholar |
Otros documentos de la autoría: Fidelak, Jeremy; Ferrer Castillo, Silvia; Oberlin, Michael; Moras, Dino; Dejaegere, Annick; Stote, Roland H.
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Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
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http://dx.doi.org/10.1007/s00249-010-0608-9 |
Metadatos
Título
Dynamic correlation networks in human peroxisome proliferator-activated receptor-γ nuclear receptor proteinAutoría
Fecha de publicación
2010Editor
Springer-VerlagISSN
0175-7571Cita bibliográfica
European Biophysics Journal (2010), 39, 11 , p. 1503-1512Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://link.springer.com/article/10.1007/s00249-010-0608-9Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
Peroxisome proliferator-activated receptor-γ nuclear receptor (PPAR-γ) belongs to the superfamily of nuclear receptor proteins that function as ligand-dependent transcription factors and plays a specific physiological ... [+]
Peroxisome proliferator-activated receptor-γ nuclear receptor (PPAR-γ) belongs to the superfamily of nuclear receptor proteins that function as ligand-dependent transcription factors and plays a specific physiological role as a regulator of lipid metabolism. A number of experimental studies have suggested that allostery plays an important role in the functioning of PPAR-γ. Here we use normal-mode analysis of PPAR-γ to characterize a network of dynamically coupled amino acids that link physiologically relevant binding surfaces such as the ligand-dependent activation domain AF-2 with the ligand binding site and the heterodimer interface. Multiple calculations were done in both the presence and absence of the agonist rosiglitazone, and the differences in dynamics were characterized. The global dynamics of the ligand binding domain were affected by the ligand, and in particular, changes to the network of dynamically correlated amino acids were observed with only small changes in conformation. These results suggest that changes in dynamic couplings can be functionally significant with respect to the transmission of allosteric signals. [-]
Derechos de acceso
(c) European Biophysical Societies’ Association 2010
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http://rightsstatements.org/vocab/InC/1.0/
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