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PDBsum entry 1sj0

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Hormone/growth factor receptor PDB id
1sj0
Jmol
Contents
Protein chain
243 a.a. *
Ligands
E4D
Waters ×152
* Residue conservation analysis
PDB id:
1sj0
Name: Hormone/growth factor receptor
Title: Human estrogen receptor alpha ligand-binding domain in compl the antagonist ligand 4-d
Structure: Estrogen receptor. Chain: a. Fragment: ligand binding domain. Synonym: er, estradiol receptor, er-alpha. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: esr1, nr3a1, esr. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PDB file)
Resolution:
1.90Å     R-factor:   0.218     R-free:   0.272
Authors: S.Kim,J.Y.Wu,E.T.Birzin,W.Chan,L.Y.Pai,Y.T.Yang,R.T.Mosley, P.M.Fitzgerald,N.Sharma,F.Dininno,S.P.Rohrer,J.M.Schaeffer, M.L.Hammond
Key ref: S.Kim et al. (2004). Estrogen receptor ligands. II. Discovery of benzoxathiins as potent, selective estrogen receptor alpha modulators. J Med Chem, 47, 2171-2175. PubMed id: 15084115 DOI: 10.1021/jm034243o
Date:
02-Mar-04     Release date:   27-Apr-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03372  (ESR1_HUMAN) -  Estrogen receptor
Seq:
Struc:
 
Seq:
Struc:
595 a.a.
243 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: 10.1021/jm034243o J Med Chem 47:2171-2175 (2004)
PubMed id: 15084115  
 
 
Estrogen receptor ligands. II. Discovery of benzoxathiins as potent, selective estrogen receptor alpha modulators.
S.Kim, J.Y.Wu, E.T.Birzin, K.Frisch, W.Chan, L.Y.Pai, Y.T.Yang, R.T.Mosley, P.M.Fitzgerald, N.Sharma, J.Dahllund, A.G.Thorsell, F.DiNinno, S.P.Rohrer, J.M.Schaeffer, M.L.Hammond.
 
  ABSTRACT  
 
The discovery and synthesis of dihydrobenzoxathiins as potent, ERalpha subtype selective ligands are described. The most active analogue, 4-D, was found to be 50-fold selective in a competitive binding assay and 100-fold selective in a transactivation assay in HEK-293 cells. The alpha selectivity was postulated to lie in the interaction of the sulfur atom of the benzoxathiin ring with the two discriminating residues in the binding pocket of the receptor isoforms.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20148675 P.Huang, V.Chandra, and F.Rastinejad (2010).
Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics.
  Annu Rev Physiol, 72, 247-272.  
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.  
18068350 V.C.Jordan (2008).
Tamoxifen: catalyst for the change to targeted therapy.
  Eur J Cancer, 44, 30-38.  
17456742 F.F.Vajdos, L.R.Hoth, K.F.Geoghegan, S.P.Simons, P.K.LeMotte, D.E.Danley, M.J.Ammirati, and J.Pandit (2007).
The 2.0 A crystal structure of the ERalpha ligand-binding domain complexed with lasofoxifene.
  Protein Sci, 16, 897-905.
PDB code: 2ouz
17518366 J.V.Turner, S.Agatonovic-Kustrin, and B.D.Glass (2007).
Molecular aspects of phytoestrogen selective binding at estrogen receptors.
  J Pharm Sci, 96, 1879-1885.  
18317942 M.Spreafico, E.Boriani, E.Benfenati, and M.Novic (2007).
Structural features of diverse ligands influencing binding affinities to estrogen alpha and estrogen beta receptors. Part II. Molecular descriptors calculated from conformation of the ligands in the complex resulting from previous docking study.
  Mol Divers, 11, 171-181.  
16914190 P.Ascenzi, A.Bocedi, and M.Marino (2006).
Structure-function relationship of estrogen receptor alpha and beta: impact on human health.
  Mol Aspects Med, 27, 299-402.  
15667591 S.Nilsson, and K.F.Koehler (2005).
Oestrogen receptors and selective oestrogen receptor modulators: molecular and cellular pharmacology.
  Basic Clin Pharmacol Toxicol, 96, 15-25.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.