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Title
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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid.
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Authors
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J.P.Renaud,
N.Rochel,
M.Ruff,
V.Vivat,
P.Chambon,
H.Gronemeyer,
D.Moras.
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Ref.
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Nature, 1995,
378,
681-689.
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PubMed id
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Abstract
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The 2.0-A crystal structure of the ligand-binding domain (LBD) of the human
retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid reveals the
ligand-binding interactions and suggests an electrostatic guidance mechanism.
The overall fold is similar to that of the human RXR-alpha apo-LBD, except for
the carboxy-terminal part which folds back towards the LBD core, contributing to
the hydrophobic ligand pocket and 'sealing' its entry site. We propose a 'mouse
trap' mechanism whereby a ligand-induced conformational transition repositions
the amphipathic alpha-helix of the AF-2 activating domain and forms a
transcriptionally active receptor.
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