ArticleEuropean biophysics journal : EBJ2010
Dynamic correlation networks in human peroxisome proliferator-activated receptor-γ nuclear receptor protein.
Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Recurrent activating mutations of PPARγ associated with luminal bladder tumors.Nature communications · 2019Article
- Post-translational modifications in DNA topoisomerase 2α highlight the role of a eukaryote-specific residue in the ATPase domain.Scientific reports · 2018Article
- The Promiscuity of Allosteric Regulation of Nuclear Receptors by Retinoid X Receptor.The journal of physical chemistry. B · 2016Article
- Allosteric Pathways in the PPARγ-RXRα nuclear receptor complex.Scientific reports · 2016Article
- Phosphorylation of PPARγ Affects the Collective Motions of the PPARγ-RXRα-DNA Complex.PloS one · 2015Article
- Article
- Multiple pathways promote dynamical coupling between catalytic domains in Escherichia coli prolyl-tRNA synthetase.Biochemistry · 2013Article
- Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
Indexed as
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Registered trials
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