1G50

CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION

Summary for 1G50

• Entry DOI: 10.2210/pdb1g50/pdb
• Related: 1qkt 1qkw
• Descriptor: ESTROGEN RECEPTOR, ESTRADIOL (3 entities in total)
• Functional Keywords: alpha helices, estradiol, structural proteomics in europe, spine, structural genomics, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Nucleus. Isoform 3: Nucleus: P03372
• Total number of polymer chains: 3
• Total formula weight: 85640.01

Authors

Eiler, S.,Gangloff, M.,Duclaud, S.,Moras, D.,Ruff, M.,Structural Proteomics in Europe (SPINE) (deposition date: 2000-10-30, release date: 2002-02-06, Last modification date: 2023-08-09)

Primary citation

Eiler, S.,Gangloff, M.,Duclaud, S.,Moras, D.,Ruff, M.
Overexpression, Purification, and Crystal Structure of Native ER alpha LBD
Protein Expr.Purif., 22:165-173, 2001

PubMed 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.

PubMed: 11437591
DOI: 10.1006/prep.2001.1409

Experimental method

X-RAY DIFFRACTION (2.9 Å)