Abstract
The structure-activity relationships of T0901317 analogs were explored as RORc inverse agonists using the principles of property- and structure-based drug design. An X-ray co-crystal structure of T0901317 and RORc was obtained and provided molecular insight into why T0901317 functioned as an inverse agonist of RORc; whereas, the same ligand functioned as an agonist of FXR, LXR, and PXR. The structural data was also used to design inhibitors with improved RORc biochemical and cellular activities. The improved inhibitors possessed enhanced selectivity profiles (rationalized using the X-ray crystallographic data) against other nuclear receptors.
Keywords:
Autoimmune; IL-17; Inflammation; RORc; RORγ; T0901317; X-ray structure.
Copyright © 2013 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Binding Sites
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Crystallography, X-Ray
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Drug Design*
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Drug Inverse Agonism
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Humans
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Hydrocarbons, Fluorinated / chemical synthesis
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Hydrocarbons, Fluorinated / chemistry
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Hydrocarbons, Fluorinated / metabolism
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Interferon-gamma / metabolism
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Interleukin-17 / metabolism
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Leukocytes, Mononuclear / drug effects
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Leukocytes, Mononuclear / metabolism
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Molecular Dynamics Simulation
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Nuclear Receptor Subfamily 1, Group F, Member 3 / agonists*
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Nuclear Receptor Subfamily 1, Group F, Member 3 / metabolism
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Propanols / chemistry*
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Protein Binding / drug effects
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Protein Structure, Tertiary
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Structure-Activity Relationship
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Sulfonamides / chemical synthesis
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Sulfonamides / chemistry*
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Sulfonamides / metabolism
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Sulfonamides / pharmacology*
Substances
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Hydrocarbons, Fluorinated
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Interleukin-17
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Nuclear Receptor Subfamily 1, Group F, Member 3
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Propanols
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Sulfonamides
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T0901317
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hexafluoroisopropanol
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Interferon-gamma