Abstract:
:Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ERβ and its domains for studying the functional analysis of ligand-protein interaction. Briefly, ERβ and its transactivation domain (TAD) and ligand binding domain (LBD) were subcloned and overexpressed using a prokaryotic expression system. The recombinant proteins were purified using Ni(+2)-IDA affinity chromatography and analyzed by NMR. Purified ERβ and TAD show similar conformation in the absence or presence of 17β-estradiol. However, LBD shows altered conformation in the presence of 17β-estradiol. These findings suggest that ERβ produced in bacteria exhibits a conformation such that its LBD remains masked and consequently it binds less to 17β-estradiol. Such study may help to develop the therapeutic approaches for controlling the estradiol-mediated gene expression in hormone dependent diseases.
journal_name
Mol Biol Repjournal_title
Molecular biology reportsauthors
Paramanik V,Thakur MKdoi
10.1007/s11033-010-0600-6subject
Has Abstractpub_date
2011-10-01 00:00:00pages
4657-61issue
7eissn
0301-4851issn
1573-4978journal_volume
38pub_type
杂志文章abstract::To explore the relationship of Notch1 mutation in T-ALL with the survival rate of T-ALL patients. The PubMed database, the Cochrane Library, conference proceedings, EMBASE databases, and references of published trials and review articles were searched. Two reviewers independently assessed the quality of the trials and...
journal_title:Molecular biology reports
pub_type: 杂志文章,meta分析,评审
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pub_type: 杂志文章,meta分析
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pub_type: 杂志文章,评审
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