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1g50
From Proteopedia
Revision as of 14:24, 28 September 2014 by OCA (Talk | contribs)
1g50 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Overexpression, purification, and crystal structure of native ER alpha LBD.,Eiler S, Gangloff M, Duclaud S, Moras D, Ruff M Protein Expr Purif. 2001 Jul;22(2):165-73. PMID:11437591[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Eiler S, Gangloff M, Duclaud S, Moras D, Ruff M. Overexpression, purification, and crystal structure of native ER alpha LBD. Protein Expr Purif. 2001 Jul;22(2):165-73. PMID:11437591 doi:10.1006/prep.2001.1409
