Related ArticlesNMR analysis on the sialic acid-binding mechanism of an R-type lectin mutant by natural evolution-mimicry.
FEBS Lett. 2016 Jun;590(12):1720-8
Authors: Hemmi H, Kuno A, Unno S, Hirabayashi J
Abstract
A sialic acid-binding lectin (SRC) was created from the C-terminal domain of an R-type N-acetyl lactosamine-binding lectin (EW29Ch) by natural evolution-mimicry. Here, we clarified its sialic acid-binding mechanism using NMR spectroscopy. The NMR analysis showed differences between conformations of the 6'-sialyllactose-bound SRC in the solution state and that in the crystal state, and differences between the internal motion of the loop region in subdomain ? in SRC and that of the corresponding region in EW29Ch. The NMR analysis thus provided useful information to explain the manner of binding to 6'-sialyllactose in solution, which the previous X-ray crystal structure analysis lacked.
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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[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):i
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Protein-ligand interactions are driven by many factors, including protein conformation and pH of the solution. Electrospray mass spectrometry can reveal the degree of protein folding from the distribution of...
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07-31-2013 12:00 PM
[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):895-903
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Human liver fatty acid binding protein (hL-FABP) is the most abundant cytosolic protein in the liver. This protein plays important roles associated to partitioning of fatty acids (FAs) to specific...
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07-31-2013 12:00 PM
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
J Mol Biol. 2011 Jul 23;
Authors: Sugimoto H, Noda Y, Segawa SI
A thermally unfolded disulfide-deficient mutant of the starch-binding domain of glucoamylase refolds into a kinetically trapped metastable intermediate when subjected to a rapid lowering of temperature. We attempted to characterise...
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08-02-2011 11:40 AM
[NMR paper] Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant n
Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant natural killer cell receptor NKR-P1A observed by NMR spectroscopy.
Related Articles Binding of sucrose octasulphate to the C-type lectin-like domain of the recombinant natural killer cell receptor NKR-P1A observed by NMR spectroscopy.
Chembiochem. 2002 Nov 4;3(11):1072-7
Authors: Kogelberg H, Frenkiel TA, Birdsall B, Chai W, Muskett FW
NKR-P1A is a C-type lectin-like receptor on natural killer cells believed to be involved in the cytotoxicity of these cells....
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11-24-2010 08:58 PM
[NMR paper] Intestinal fatty acid binding protein: the folding mechanism as determined by NMR stu
Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Related Articles Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Biochemistry. 2001 Jan 23;40(3):732-42
Authors: Hodsdon ME, Frieden C
The intestinal fatty acid binding protein is composed of two beta-sheets surrounding a large interior cavity. There is a small helical domain associated with the portal for entry of the ligand into the cavity. Denaturation of the protein has been monitored in a residue-specific...
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11-19-2010 08:32 PM
[NMR paper] NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoi
NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoic acid binding protein.
Related Articles NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoic acid binding protein.
Biochim Biophys Acta. 1999 Aug 17;1433(1-2):240-52
Authors: Wang L, Yan H
Cellular RA binding proteins are thought to play important roles in the (RA), a hormonally active metabolite of vitamin A that has profound effects on cell growth, + differentiation and morphogenesis. Binding of RA to type II human cellular...
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11-18-2010 08:31 PM
[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Biochemistry. 1998 Sep 15;37(37):12727-36
Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
NMR analysis on the sialic acid-binding mechanism of an R-type lectin mutant by natural evolution-mimicry.
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