PDBsum entry 2nv7

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protein ligands Protein-protein interface(s) links
Transcription PDB id
Protein chains
228 a.a. *
555 ×2
Waters ×246
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Crystal structure of estrogen receptor beta complexed with way-555
Structure: Estrogen receptor beta. Chain: a, b. Synonym: er-beta. Engineered: yes. Nuclear receptor coactivator 1. Chain: c, d. Synonym: ncoa-1, steroid receptor coactivator 1, src-1, rip160, protein hin-2, ny-ren-52 antigen. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: esr2, estrb, nr3a2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence was derived from steroid receptor coactivator-1
2.10Å     R-factor:   0.211     R-free:   0.265
Authors: R.E.Mewshaw,M.S.Bowen,H.A.Harris,Z.B.Xu,E.S.Manas,S.T.Cohn, Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: R.E.Mewshaw et al. (2007). ERbeta ligands. Part 5: synthesis and structure-activity relationships of a series of 4'-hydroxyphenyl-aryl-carbaldehyde oxime derivatives. Bioorg Med Chem Lett, 17, 902-906. PubMed id: 17188490 DOI: 10.1016/j.bmcl.2006.11.066
10-Nov-06     Release date:   21-Aug-07    
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Protein chains
Pfam   ArchSchema ?
Q92731  (ESR2_HUMAN) -  Estrogen receptor beta
530 a.a.
228 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.bmcl.2006.11.066 Bioorg Med Chem Lett 17:902-906 (2007)
PubMed id: 17188490  
ERbeta ligands. Part 5: synthesis and structure-activity relationships of a series of 4'-hydroxyphenyl-aryl-carbaldehyde oxime derivatives.
R.E.Mewshaw, S.M.Bowen, H.A.Harris, Z.B.Xu, E.S.Manas, S.T.Cohn.
A series of 4'-hydroxyphenyl-aryl-carbaldehyde oximes (5b) was prepared and found to have high affinity (4nM) and modest selectivity (39-fold) for estrogen receptor-beta (ERbeta). Substitution of one of the core rings of the scaffold based around these novel ligands further expanded our knowledge in the quest toward achieving high affinity and selectivity for ERbeta. An X-ray co-crystal of structure 11 revealed that the oxime moiety was mimicking the C-ring of genistein, as previously predicted by SAR and docking studies.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  19967775 F.Minutolo, M.Macchia, B.S.Katzenellenbogen, and J.A.Katzenellenbogen (2011).
Estrogen receptor β ligands: recent advances and biomedical applications.
  Med Res Rev, 31, 364-442.  
21481497 S.Bertini, A.De Cupertinis, C.Granchi, B.Bargagli, T.Tuccinardi, A.Martinelli, M.Macchia, J.R.Gunther, K.E.Carlson, J.A.Katzenellenbogen, and F.Minutolo (2011).
Selective and potent agonists for estrogen receptor beta derived from molecular refinements of salicylaldoximes.
  Eur J Med Chem, 46, 2453-2462.  
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