Abstract
The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Biopolymers
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Computer Graphics
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Crystallography, X-Ray
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DNA / metabolism
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Escherichia coli
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Humans
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Ligands
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Models, Molecular
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Molecular Sequence Data
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Nuclear Proteins / metabolism
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Receptors, Retinoic Acid / chemistry*
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Receptors, Retinoic Acid / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Retinoid X Receptors
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Transcription Factors / chemistry*
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Transcription Factors / metabolism
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Transcriptional Activation
Substances
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Biopolymers
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Ligands
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Nuclear Proteins
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Receptors, Retinoic Acid
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Recombinant Proteins
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Retinoid X Receptors
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Transcription Factors
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DNA