Abstract
Aldo-keto reductase 1a4 (AKR1a4; EC 1.1.1.2) is the mouse orthologue of human aldehyde reductase (AKR1a1), the founding member of the AKR family. As an NADPH-dependent enzyme, AKR1a4 catalyses the conversion of D-glucuronate to L-gulonate. AKR1a4 is involved in ascorbate biosynthesis in mice, but has also recently been found to interact with SMAR1, providing a novel mechanism of ROS regulation by ATM. Here, the crystal structure of AKR1a4 in its apo form at 1.64 Å resolution as well as the characterization of the binding of AKR1a4 to NADPH and P44, a peptide derived from SMAR1, is presented.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehyde Reductase / chemistry*
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Amino Acid Sequence
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Animals
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Apoenzymes / chemistry
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Calorimetry
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Cell Cycle Proteins / chemistry
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Crystallography, X-Ray
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DNA-Binding Proteins / chemistry
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Ligands
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Mice
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Models, Molecular
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Molecular Sequence Data
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Nuclear Proteins / chemistry
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Peptide Fragments / chemistry
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Structural Homology, Protein
Substances
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Apoenzymes
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Banp protein, mouse
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Cell Cycle Proteins
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DNA-Binding Proteins
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Ligands
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Nuclear Proteins
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Peptide Fragments
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Akr1a1 protein, mouse
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Aldehyde Reductase