PDBsum entry 2zas

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Transcription PDB id
Protein chain
227 a.a. *
Waters ×149
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Crystal structure of human estrogen-related receptor gamma l binding domain complex with 4-alpha-cumylphenol, a bispheno derivative
Structure: Estrogen-related receptor gamma. Chain: a. Fragment: ligand binding domain, unp residues 222-459. Synonym: estrogen receptor-related protein 3, err gamma-2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
2.00Å     R-factor:   0.212     R-free:   0.237
Authors: A.Matsushima,Y.Kakuta,T.Teramoto,Y.Shimohigashi
Key ref: A.Matsushima et al. (2008). ERRgamma tethers strongly bisphenol A and 4-alpha-cumylphenol in an induced-fit manner. Biochem Biophys Res Commun, 373, 408-413. PubMed id: 18582436 DOI: 10.1016/j.bbrc.2008.06.050
09-Oct-07     Release date:   07-Oct-08    
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Protein chain
Pfam   ArchSchema ?
P62508  (ERR3_HUMAN) -  Estrogen-related receptor gamma
458 a.a.
227 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     steroid hormone mediated signaling pathway   2 terms 
  Biochemical function     DNA binding     4 terms  


DOI no: 10.1016/j.bbrc.2008.06.050 Biochem Biophys Res Commun 373:408-413 (2008)
PubMed id: 18582436  
ERRgamma tethers strongly bisphenol A and 4-alpha-cumylphenol in an induced-fit manner.
A.Matsushima, T.Teramoto, H.Okada, X.Liu, T.Tokunaga, Y.Kakuta, Y.Shimohigashi.
A receptor-binding assay and X-ray crystal structure analysis demonstrated that the endocrine disruptor bisphenol A (BPA) strongly binds to human estrogen-related receptor gamma (ERRgamma). BPA is well anchored to the ligand-binding pocket, forming hydrogen bonds with its two phenol-hydroxyl groups. In this study, we found that 4-alpha-cumylphenol lacking one of its phenol-hydroxyl groups also binds to ERRgamma very strongly. The 2.0 A crystal structure of the 4-alpha-cumylphenol/ERRgamma complex clearly revealed that ERRgamma's Leu345-beta-isopropyl plays a role in the tight binding of 4-alpha-cumylphenol and BPA, rotating in a back-and-forth induced-fit manner.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21196344 J.C.Robins, C.J.Marsit, J.F.Padbury, and S.S.Sharma (2011).
Endocrine disruptors, environmental oxygen, epigenetics and pregnancy.
  Front Biosci (Elite Ed), 3, 690-700.  
21234470 S.Ardizzone, G.Cappelletti, D.Meroni, and F.Spadavecchia (2011).
Tailored TiO2 layers for the photocatalytic ozonation of cumylphenol, a refractory pollutant exerting hormonal activity.
  Chem Commun (Camb), 47, 2640-2642.  
  20427257 A.Matsushima, X.Liu, H.Okada, M.Shimohigashi, and Y.Shimohigashi (2010).
Bisphenol AF is a full agonist for the estrogen receptor ERalpha but a highly specific antagonist for ERbeta.
  Environ Health Perspect, 118, 1267-1272.  
20063036 A.le Maire, W.Bourguet, and P.Balaguer (2010).
A structural view of nuclear hormone receptor: endocrine disruptor interactions.
  Cell Mol Life Sci, 67, 1219-1237.
PDB code: 3kwy
20542892 X.Liu, A.Matsushima, H.Okada, and Y.Shimohigashi (2010).
Distinction of the binding modes for human nuclear receptor ERRgamma between bisphenol A and 4-hydroxytamoxifen.
  J Biochem, 148, 247-254.  
19433248 B.S.Rubin, and A.M.Soto (2009).
Bisphenol A: Perinatal exposure and body weight.
  Mol Cell Endocrinol, 304, 55-62.  
19535786 H.B.Adewale, W.N.Jefferson, R.R.Newbold, and H.B.Patisaul (2009).
Neonatal bisphenol-a exposure alters rat reproductive development and ovarian morphology without impairing activation of gonadotropin-releasing hormone neurons.
  Biol Reprod, 81, 690-699.  
19304792 Y.Takeda, X.Liu, M.Sumiyoshi, A.Matsushima, M.Shimohigashi, and Y.Shimohigashi (2009).
Placenta expressing the greatest quantity of bisphenol A receptor ERR{gamma} among the human reproductive tissues: Predominant expression of type-1 ERR{gamma} isoform.
  J Biochem, 146, 113-122.  
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