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3d6d
From Proteopedia
Contents |
Crystal Structure of the complex between PPARgamma LBD and the LT175(R-enantiomer)
Template:ABSTRACT PUBMED 19053776
About this Structure
3d6d is a 2 chain structure of Peroxisome Proliferator-Activated Receptors with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Montanari R, Saccoccia F, Scotti E, Crestani M, Godio C, Gilardi F, Loiodice F, Fracchiolla G, Laghezza A, Tortorella P, Lavecchia A, Novellino E, Mazza F, Aschi M, Pochetti G. Crystal structure of the peroxisome proliferator-activated receptor gamma (PPARgamma) ligand binding domain complexed with a novel partial agonist: a new region of the hydrophobic pocket could be exploited for drug design. J Med Chem. 2008 Dec 25;51(24):7768-76. PMID:19053776 doi:10.1021/jm800733h
- Pochetti G, Godio C, Mitro N, Caruso D, Galmozzi A, Scurati S, Loiodice F, Fracchiolla G, Tortorella P, Laghezza A, Lavecchia A, Novellino E, Mazza F, Crestani M. Insights into the mechanism of partial agonism: crystal structures of the peroxisome proliferator-activated receptor gamma ligand-binding domain in the complex with two enantiomeric ligands. J Biol Chem. 2007 Jun 8;282(23):17314-24. Epub 2007 Apr 2. PMID:17403688 doi:10.1074/jbc.M702316200
- Bruning JB, Chalmers MJ, Prasad S, Busby SA, Kamenecka TM, He Y, Nettles KW, Griffin PR. Partial agonists activate PPARgamma using a helix 12 independent mechanism. Structure. 2007 Oct;15(10):1258-71. PMID:17937915 doi:http://dx.doi.org/10.1016/j.str.2007.07.014
- Gampe RT Jr, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE. Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55. PMID:10882139
Categories: Homo sapiens | Montanari, R. | Pochetti, G. | Activator | Alternative splicing | Bundle of alpha-helices and a small four-stranded beta-sheet | Diabetes mellitus | Disease mutation | Dna-binding | Metal-binding | Nucleus | Obesity | Phosphoprotein | Polymorphism | Receptor | Transcription | Transcription regulation | Zinc | Zinc-finger
