3hq5 | pdb_00003hq5

Progesterone Receptor bound to an Alkylpyrrolidine ligand.

spinqualitylabelsall models 3hq5, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hq5 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GKK, GOL, SO4 Gene: PGR, NR3C3 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PRGR_HUMAN] The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation. Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Using the X-ray crystal structure of an amide-based progesterone receptor (PR) partial agonist bound to the PR ligand binding domain, a novel PR partial agonist class containing a pyrrolidine ring was designed. Members of this class of N-alkylpyrrolidines demonstrate potent and highly selective partial agonism of the progesterone receptor, and one of these analogs was shown to be efficacious upon oral dosing in the OVX rat model of estrogen opposition. Rational design of orally-active, pyrrolidine-based progesterone receptor partial agonists.,Thompson SK, Washburn DG, Frazee JS, Madauss KP, Hoang TH, Lapinski L, Grygielko ET, Glace LE, Trizna W, Williams SP, Duraiswami C, Bray JD, Laping NJ Bioorg Med Chem Lett. 2009 Aug 15;19(16):4777-80. Epub 2009 Jun 17. PMID:19595590 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hormone

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