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PDBsum entry 2jj3

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protein ligands Protein-protein interface(s) links
Transcription PDB id
2jj3
Jmol PyMol
Contents
Protein chains
224 a.a. *
Ligands
JJ3 ×2
Waters ×62
* Residue conservation analysis
PDB id:
2jj3
Name: Transcription
Title: Estrogen receptor beta ligand binding domain in complex with a benzopyran agonist
Structure: Estrogen receptor beta. Chain: a, b. Fragment: ligand-binding domain, residues 256-505. Synonym: er-beta. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.28Å     R-factor:   0.235     R-free:   0.255
Authors: B.H.Norman,T.I.Richardson,J.A.Dodge,L.A.Pfeifer,G.L.Durst, Y.Wang,J.D.Durbin,V.Krishnan,S.R.Dinn,S.Liu,J.E.Reilly, K.T.Ryter
Key ref: B.H.Norman et al. (2007). Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 4: functionalization of the benzopyran A-ring. Bioorg Med Chem Lett, 17, 5082-5085. PubMed id: 17662603 DOI: 10.1016/j.bmcl.2007.07.009
Date:
03-Jul-07     Release date:   07-Aug-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q92731  (ESR2_HUMAN) -  Estrogen receptor beta
Seq:
Struc:
 
Seq:
Struc:
530 a.a.
224 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     3 terms  

 

 
DOI no: 10.1016/j.bmcl.2007.07.009 Bioorg Med Chem Lett 17:5082-5085 (2007)
PubMed id: 17662603  
 
 
Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 4: functionalization of the benzopyran A-ring.
B.H.Norman, T.I.Richardson, J.A.Dodge, L.A.Pfeifer, G.L.Durst, Y.Wang, J.D.Durbin, V.Krishnan, S.R.Dinn, S.Liu, J.E.Reilly, K.T.Ryter.
 
  ABSTRACT  
 
Benzopyrans are selective estrogen receptor (ER) beta agonists (SERBAs), which bind the ER receptor subtypes alpha and beta in opposite orientations. We have used structure based drug design to show that this unique phenomena can be exploited via substitution at the 8-position of the benzopyran A-ring to disrupt binding to ERalpha, thus improving ERbeta subtype selectivity. X-ray cocrystal structures with ERalpha and ERbeta are supportive of this approach to improve selectivity in this structural class.
 

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.  
19063592 A.Amadasi, A.Mozzarelli, C.Meda, A.Maggi, and P.Cozzini (2009).
Identification of xenoestrogens in food additives by an integrated in silico and in vitro approach.
  Chem Res Toxicol, 22, 52-63.  
18989626 H.Shadnia, J.S.Wright, and J.M.Anderson (2009).
Interaction force diagrams: new insight into ligand-receptor binding.
  J Comput Aided Mol Des, 23, 185-194.  
  19293997 J.P.Salisbury, and J.C.Williams (2009).
Docking study of triphenylphosphonium cations as estrogen receptor alpha modulators.
  Bioinformation, 3, 303-307.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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