1g50
From Proteopedia
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| - | [[Image:1g50.gif|left|200px]] | + | [[Image:1g50.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION''' | + | {{Structure |
| + | |PDB= 1g50 |SIZE=350|CAPTION= <scene name='initialview01'>1g50</scene>, resolution 2.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=EST:ESTRADIOL'>EST</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G50 is a [ | + | 1G50 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G50 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11437591 11437591] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: EST]] | [[Category: EST]] | ||
| - | [[Category: alpha | + | [[Category: alpha helice]] |
[[Category: estradiol]] | [[Category: estradiol]] | ||
[[Category: spine]] | [[Category: spine]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:16 2008'' |
Revision as of 09:18, 20 March 2008
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| , resolution 2.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A WILD TYPE HER ALPHA LBD AT 2.9 ANGSTROM RESOLUTION
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Atherosclerosis, susceptibility to OMIM:[133430], Breast cancer OMIM:[133430], Estrogen resistance OMIM:[133430], HDL response to hormone replacement, augmented OMIM:[133430], Migraine, susceptibility to OMIM:[133430], Myocardial infarction, susceptibility to OMIM:[133430]
About this Structure
1G50 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:18:16 2008
