Related ArticlesThermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase.
Biochem Biophys Res Commun. 2015 Oct 27;
Authors: Qin S, Shimamoto S, Maruno T, Kobayashi Y, Kawahara K, Yoshida T, Ohkubo T
Abstract
Lipocalin-type prostaglandin D synthase (L-PGDS) is one of the most abundant proteins in human cerebrospinal fluid (CSF) with dual functions as a prostaglandin D2 (PGD2) synthase and a transporter of lipophilic ligands. Recent studies revealed that L-PGDS plays important roles in protecting against various neuronal diseases induced by reactive oxygen species (ROS). However, the molecular mechanisms of such protective actions of L-PGDS remain unknown. In this study, we conducted thermodynamic and nuclear magnetic resonance (NMR) analyses, and demonstrated that L-PGDS binds to nicotinamide coenzymes, including NADPH, NADP(+), and NADH. Although a hydrophilic ligand is not common for L-PGDS, these ligands, especially NADPH showed specific interaction with L-PGDS at the upper pocket of its ligand-binding cavity with an unusually bifurcated shape. The binding affinity of L-PGDS for NADPH was comparable to that previously reported for NADPH oxidases and NADPH in vitro. These results suggested that L-PGDS potentially attenuates the activities of NADPH oxidases through interaction with NADPH. Given that NADPH is the substrate for NADPH oxidases that play key roles in neuronal cell death by generating excessive ROS, these results imply a novel linkage between L-PGDS and ROS.
PMID: 26518650 [PubMed - as supplied by publisher]
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Abstract
Antifreeze proteins (AFPs) are found in a variety of cold-adapted (psychrophilic) organisms to promote survival at subzero temperatures by binding to ice crystals and decreasing the freezing temperature of body fluids. The type III AFPs are small globular proteins that consist of one α-helix, three 310-helices, and two β-strands. Sialic acids play important roles in a variety of biological functions, such as...
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01-09-2015 03:58 PM
[NMR paper] Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
Biochim Biophys Acta. 2013 Jul 16;
Authors: Létourneau D, Lorin A, Lefebvre A, Cabana J, Lavigne P, Lehoux JG
Abstract
STARD5 is a member of the STARD4 sub-family...
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07-23-2013 09:52 PM
[NMR paper] Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Related Articles Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
J Biol Chem. 2013 Jun 20;
Authors: Probert F, Whittaker SB, Crispin M, Mitchell DA, Dixon AM
Abstract
The C-type lectin DC-SIGNR (Dendritic Cell-Specific ICAM-3-Grabbing...
Thermodynamic and NMR analysis of inhibitor binding to dihydrofolate reductase.
Thermodynamic and NMR analysis of inhibitor binding to dihydrofolate reductase.
Thermodynamic and NMR analysis of inhibitor binding to dihydrofolate reductase.
Bioorg Med Chem. 2010 Dec 15;18(24):8485-92
Authors: Batruch I, Javasky E, Brown ED, Organ MG, Johnson PE
Isothermal titration calorimetry (ITC) was used to determine the thermodynamic driving force for inhibitor binding to the enzyme dihydrofolate reductase (DHFR) from Escherichia coli. 1,4-Bis-{sulfanylmethyl}-3,6-dimethyl-benzene (1) binds DHFR:NADPH with a K(d) of 13±5 nM while the...
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03-09-2011 02:20 PM
NMR assignment of 1H, 13C, and 15N resonances of rat lipocalin-type prostaglandin D synthase.
NMR assignment of 1H, 13C, and 15N resonances of rat lipocalin-type prostaglandin D synthase.
NMR assignment of 1H, 13C, and 15N resonances of rat lipocalin-type prostaglandin D synthase.
Biomol NMR Assign. 2010 Oct;4(2):223-5
Authors: Liu J, Lv Y, Guo C, Lin D
Lipocalin-type prostaglandin D synthase (L-PGDS) acts as both a PGD(2)-synthesizing enzyme and an extracellular transporter for small lipophilic molecules. Here we report the backbone and side-chain resonance assignments of uniformly (15)N, (13)C labeled rat L-PGDS.
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03-05-2011 01:02 PM
NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the c
NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1).
Related Articles NMR analyses of the G{beta}{gamma} binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1).
J Biol Chem. 2010 Nov 12;
Authors: Yokogawa M, Osawa M, Takeuchi K, Mase Y, Shimada I
G protein-activated inwardly rectifying potassium channel (GIRK) plays crucial roles in regulating heart...