NDLI: Structural modeling of high-affinity thyroid receptor

Content Provider	Springer Nature Link
Author	Araujo, Alexandre Suman Martínez, Leandro Paula Nicoluci, Ricardo Skaf, Munir S. Polikarpov, Igor
Copyright Year	2010
Abstract	Understanding the molecular basis of the binding modes of natural and synthetic ligands to nuclear receptors is fundamental to our comprehension of the activation mechanism of this important class of hormone regulated transcription factors and to the development of new ligands. Thyroid hormone receptors (TR) are particularly important targets for pharmaceuticals development because TRs are associated with the regulation of metabolic rates, body weight, and circulating levels of cholesterol and triglycerides in humans. While several high-affinity ligands are known, structural information is only partially available. In this work we obtain structural models of several TR–ligand complexes with unknown structure by docking high affinity ligands to the receptors’ ligand binding domain with subsequent relaxation by molecular dynamics simulations. The binding modes of these ligands are discussed providing novel insights into the development of TR ligands. The experimental binding free energies are reasonably well-reproduced from the proposed models using a simple linear interaction energy free-energy calculation scheme.
Starting Page	1523
Ending Page	1536
Page Count	14
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	39
Issue Number	11
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2010-05-30
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Molecular dynamics Nuclear receptor Binding free energy Thyroid hormone receptor Thyromimetics-receptor binding modes High affinity thyromimetics Nanotechnology Neurobiology Membrane Biology Cell Biology Biophysics and Biological Physics Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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