NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Mol Biol Rep. 2010 Dec 12;
Authors: Paramanik V, Thakur MK
Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction. Briefly, ER? 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 ER? and TAD show similar conformation in the absence or presence of 17?-estradiol. However, LBD shows altered conformation in the presence of 17?-estradiol. These findings suggest that ER? produced in bacteria exhibits a conformation such that its LBD remains masked and consequently it binds less to 17?-estradiol. Such study may help to develop the therapeutic approaches for controlling the estradiol-mediated gene expression in hormone dependent diseases.
PMID: 21153770 [PubMed - as supplied by publisher]
[NMR paper] Solid-state NMR analysis of ligand--receptor interactions reveals an induced misfit i
Solid-state NMR analysis of ligand--receptor interactions reveals an induced misfit in the binding site of isorhodopsin.
Related Articles Solid-state NMR analysis of ligand--receptor interactions reveals an induced misfit in the binding site of isorhodopsin.
Biochemistry. 2004 Dec 28;43(51):16011-8
Authors: Creemers AF, Bovee-Geurts PH, DeGrip WJ, Lugtenburg J, de Groot HJ
Rhodopsin is the photosensitive protein of the rod photoreceptor in the vertebrate retina and is a paradigm for the superfamily of G-protein-coupled receptors (GPCRs)....
nmrlearner
Journal club
0
11-24-2010 10:03 PM
[NMR paper] Detection of a conformational change in maltose binding protein by (129)Xe NMR spectr
Detection of a conformational change in maltose binding protein by (129)Xe NMR spectroscopy.
Related Articles Detection of a conformational change in maltose binding protein by (129)Xe NMR spectroscopy.
J Am Chem Soc. 2001 Sep 5;123(35):8616-7
Authors: Rubin SM, Spence MM, Dimitrov IE, Ruiz EJ, Pines A, Wemmer DE
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Backbone dynamics of a bacterially expressed peptide from the receptor binding domain
Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy.
Related Articles Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy.
J Biomol NMR. 2000 Jul;17(3):239-55
Authors: Campbell AP, Spyracopoulos L, Irvin RT, Sykes BD
The backbone dynamics of a 15N-labeled recombinant PAK pilin peptide spanning residues...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] NMR structure of free RGS4 reveals an induced conformational change upon binding Galp
NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha.
Related Articles NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha.
Biochemistry. 2000 Jun 20;39(24):7063-73
Authors: Moy FJ, Chanda PK, Cockett MI, Edris W, Jones PG, Mason K, Semus S, Powers R
Heterotrimeric guanine nucleotide-binding proteins (G-proteins) are transducers in many cellular transmembrane signaling systems where regulators of G-protein signaling (RGS) act as attenuators of the G-protein signal cascade...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] Irreversible conformational change of bacterio-opsin induced by binding of retinal du
Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.
Related Articles Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.
J Biochem. 2000 May;127(5):861-9
Authors: Yamaguchi S, Tuzi S, Tanio M, Naito A, Lanyi JK, Needleman R, Saitô H
We compared (13)C NMR spectra of Ala- and Val-labeled bacterio-opsin (bO), produced either by bleaching bR...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
NMR evidence of GM1-induced conformational change of substance P using isotropic bice
NMR evidence of GM1-induced conformational change of substance P using isotropic bicelles.
Related Articles NMR evidence of GM1-induced conformational change of substance P using isotropic bicelles.
Biochim Biophys Acta. 2010 Oct 8;
Authors: Gayen A, Goswami SK, Mukhopadhyay C
Substance P (SP) is one of the target neurotransmitters associated with diseases related to chronic inflammation, pain and depression. The selective receptor for SP, NK(1)R is located in the heterogeneous microdomains or caveolaes in membrane. Gangliosides, specifically...
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli.
Linear Mode
