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PDBsum entry 1g50

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protein ligands Protein-protein interface(s) links
DNA binding protein PDB id
1g50
Jmol
Contents
Protein chains
247 a.a. *
Ligands
EST ×3
Waters ×165
* Residue conservation analysis
PDB id:
1g50
Name: DNA binding protein
Title: Crystal structure of a wild type her alpha lbd at 2.9 angstrom resolution
Structure: Estrogen receptor. Chain: a, b, c. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
2.90Å     R-factor:   0.241     R-free:   0.310
Authors: S.Eiler,M.Gangloff,S.Duclaud,D.Moras,M.Ruff,Structural Proteomics In Europe (Spine)
Key ref: S.Eiler et al. (2001). Overexpression, purification, and crystal structure of native ER alpha LBD. Protein Expr Purif, 22, 165-173. PubMed id: 11437591 DOI: 10.1006/prep.2001.1409
Date:
30-Oct-00     Release date:   06-Feb-02    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P03372  (ESR1_HUMAN) -  Estrogen receptor
Seq:
Struc:
 
Seq:
Struc:
595 a.a.
247 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: 10.1006/prep.2001.1409 Protein Expr Purif 22:165-173 (2001)
PubMed id: 11437591  
 
 
Overexpression, purification, and crystal structure of native ER alpha LBD.
S.Eiler, M.Gangloff, S.Duclaud, D.Moras, M.Ruff.
 
  ABSTRACT  
 
Several crystal structures of human estrogen receptor alpha ligand-binding domain (hERalpha LBD) complexed with agonist or antagonist molecules have previously been solved. The proteins had been modified in cysteine residues (carboxymethylation) or renatured in urea to circumvent aggregation and denaturation problems. In this work, high-level protein expression and purification together with crystallization screening procedure yielded high amounts of soluble protein without renaturation or modifications steps. The native protein crystallizes in the space group P3(2) 21 with three molecules in the asymmetric unit. The overall structure is very similar to that previously reported for the hERalpha LBD with cysteine carboxymethylated residues thus validating the modification approach. The present strategy can be adapted to other cases where the solubility and the proper folding is a difficulty.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21327625 P.Fechner, F.Pröll, C.Albrecht, and G.Gauglitz (2011).
Kinetic analysis of the estrogen receptor alpha using RIfS.
  Anal Bioanal Chem, 400, 729-735.  
20628447 N.Jonker, H.Lingeman, and H.Irth (2010).
Direct Dynamic Protein-Affinity Selection Mass-Spectrometry.
  Chromatographia, 72, 7.  
18767177 A.Bolli, P.Galluzzo, P.Ascenzi, G.Del Pozzo, I.Manco, M.T.Vietri, L.Mita, L.Altucci, D.G.Mita, and M.Marino (2008).
Laccase treatment impairs bisphenol A-induced cancer cell proliferation affecting estrogen receptor alpha-dependent rapid signals.
  IUBMB Life, 60, 843-852.  
18236033 J.Reinen, J.Kool, and N.P.Vermeulen (2008).
Reversed-phase liquid chromatography coupled on-line to estrogen receptor bioaffinity detection based on fluorescence polarization.
  Anal Bioanal Chem, 390, 1987-1998.  
  18097104 V.Cura, M.Gangloff, S.Eiler, D.Moras, and M.Ruff (2008).
Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ERalpha in complex with synthetic ligands.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 54-57.  
17459883 A.Lorin, B.Charloteaux, Y.Fridmann-Sirkis, A.Thomas, Y.Shai, and R.Brasseur (2007).
Mode of membrane interaction and fusogenic properties of a de novo transmembrane model peptide depend on the length of the hydrophobic core.
  J Biol Chem, 282, 18388-18396.  
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.  
16351736 P.D'Ursi, E.Salvi, P.Fossa, L.Milanesi, and E.Rovida (2005).
Modelling the interaction of steroid receptors with endocrine disrupting chemicals.
  BMC Bioinformatics, 6, S10.  
12077320 R.L.Rich, L.R.Hoth, K.F.Geoghegan, T.A.Brown, P.K.LeMotte, S.P.Simons, P.Hensley, and D.G.Myszka (2002).
Kinetic analysis of estrogen receptor/ligand interactions.
  Proc Natl Acad Sci U S A, 99, 8562-8567.  
11607933 U.Egner, N.Heinrich, M.Ruff, M.Gangloff, A.Mueller-Fahrnow, and J.M.Wurtz (2001).
Different ligands-different receptor conformations: modeling of the hER alpha LBD in complex with agonists and antagonists.
  Med Res Rev, 21, 523-539.  
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.