6lit | pdb_00006lit

Estrogen-related receptor beta(ERR2) in complex with BPA

spinqualitylabelsall models 6lit, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lit is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: 2OH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease ERR2_HUMAN Defects in ESRRB are the cause of deafness autosomal recessive type 35 (DFNB35) [MIM:608565. DFNB35 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. Function ERR2_HUMAN Nuclear receptor, may regulate ESR1 transcriptional activity. Publication Abstract from PubMed Estrogen-related receptor beta (ERRbeta) is a nuclear receptor critical for many biological processes. Despite the biological and pharmaceutical importance of ERRbeta, deciphering the structure of ERRbeta has been hampered by the difficulties in obtaining a pure and stable protein for structural studies. In fact, the ERRbeta ligand-binding domain remains the last unsolved ERR structure and also one of only a few unknown nuclear receptor structures. Here, we report the identification of a critical single-residue mutation resulted in robust solubility and stability of an active ERRbeta ligand-binding domain, thereby providing a protein tool enabling the first probe into the biochemical and structural studies of this important receptor. The crystal structure reveals key structural features that have enabled the integration of the molecular determinants of signals transduced across the ligand binding and coregulator recruitment by all three ERR subtypes, which also provides a framework for the rational design of selective and potent ligands for the treatment of various ERR-mediated diseases. Structural Insights into the Specificity of Ligand Binding and Coactivator Assembly by Estrogen-Related Receptor beta.,Yao B, Zhang S, Wei Y, Tian S, Lu Z, Jin L, He Y, Xie W, Li Y J Mol Biol. 2020 Sep 4;432(19):5460-5472. doi: 10.1016/j.jmb.2020.08.007. Epub, 2020 Aug 12. PMID:32795533 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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