4gac

High resolution structure of mouse aldehyde reductase (AKR1a4) in its apo-form

spinqualitylabelsall models 4gac, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gac is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, FLC Gene: Akr1a1, Akr1a4 (LK3 transgenic mice) Activity: Alcohol dehydrogenase (NADP(+)), with EC number 1.1.1.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AK1A1_MOUSE] Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Publication Abstract from PubMed 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 A resolution as well as the characterization of the binding of AKR1a4 to NADPH and P44, a peptide derived from SMAR1, is presented. High-resolution structure of AKR1a4 in the apo form and its interaction with ligands.,Faucher F, Jia Z Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1271-4., doi: 10.1107/S1744309112037128. Epub 2012 Oct 26. PMID:23143230 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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