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Fluorescent-labeled estrogen recepto...

Tamrazi, Anobel.

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Fluorescent-labeled estrogen receptors: Molecular sensors of receptor structure and function.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Fluorescent-labeled estrogen receptors: Molecular sensors of receptor structure and function./
作者:	Tamrazi, Anobel.
面頁冊數:	153 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1235.
Contained By:	Dissertation Abstracts International64-03B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3086195

Fluorescent-labeled estrogen receptors: Molecular sensors of receptor structure and function.
Tamrazi, Anobel.

Fluorescent-labeled estrogen receptors: Molecular sensors of receptor structure and function. - 153 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1235.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.

Estrogen receptor (ER) is one of the 48 nuclear hormone receptor (NHRs) identified in the human genome; these receptors function predominantly as ligand-regulated transcription factors. The crystallographic ER ligand binding domain (LBD) data have clearly illustrated at the atomic level the critical nature of ligand-induced receptor LBD conformations, leading to the observed pharmacological profiles of ER-ligands. Here we describe a biophysical approach to study ER structure and function.Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Fluorescent-labeled estrogen receptors: Molecular sensors of receptor structure and function.
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245 1 0 $a Fluorescent-labeled estrogen receptors: Molecular sensors of receptor structure and function.
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500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1235.
500 $a Adviser: John A. Katzenellenbogen.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.
520 $a Estrogen receptor (ER) is one of the 48 nuclear hormone receptor (NHRs) identified in the human genome; these receptors function predominantly as ligand-regulated transcription factors. The crystallographic ER ligand binding domain (LBD) data have clearly illustrated at the atomic level the critical nature of ligand-induced receptor LBD conformations, leading to the observed pharmacological profiles of ER-ligands. Here we describe a biophysical approach to study ER structure and function.
520 $a We have prepared single reactive-cysteine containing ERalpha-LBD constructs that are functionally active and can be site-specifically fluorophore-labeled at either cysteine 417 or 530. Using convenient fluorescence resonance energy transfer (FRET)-based methods we have measured the thermodynamic and kinetic stability of fluorescent-labeled ERalpha-LBD dimers. Each class of ligand pharmacological character was found to have a characteristic effect on the rate of dimer dissociation.
520 $a Several fluorescence techniques were utilized as novel biophysical approaches to monitor the conformations and conformational dynamics of the fluorescent-labeled ERalpha-LBDs. These new methods enabled us to dissect those ER structural features that are controlled by and thereby predictive of the pharmacological character of ligand, and they revealed that apo receptor has unique molten globule structural characteristics with the pharmacological nature of the ligands that bind the receptor stabilizing specific positions of helix 12 in the receptor.
520 $a Using FRET, we found that coactivator peptides increase the kinetic stability of agonist-bound ER dimers. Our fluorescence anisotropy and pyrene excimer-based results suggest that there is a coactivator regulated selective allosteric stabilization of agonist-receptor conformation and that there is a novel conformation of receptor within an agonist·ER-LBD·coactivator tripartite complex. These results suggest that coactivator peptides might behave as tissue-specific allosteric ligands of ER.
520 $a By attaching the fluorophore directly onto the ligand-binding domain, we have created out of the ER a molecular sensor through which we can probe directly the conformational state of the receptor with high sensitivity. Thus, fluorophore-labeled ERs provide tools for studying receptor structure and function that nicely complement x-ray crystallography and NMR spectroscopy.
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791 $a Ph.D.
792 $a 2003
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