Related ArticlesImpact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics.
Biochemistry. 2013 Jan 25;
Authors: Nowakowski ME, Ruszczynska-Bartnik K, Budzinska M, Jaremko L, Jaremko M, Zdanowski K, Bierzynski AJ, Ejchart A
Abstract
S100 proteins play a crucial role in multiple important biological processes in vertebrate organisms acting predominantly as calcium signal transmitters. S100A1 is a typical representative of this family of proteins. Upon binding of four Ca2+ ions it undergoes a dramatic conformational change, resulting in exposure, in each of its two identical subunits, a large hydrophobic cleft that binds to target proteins. It has been shown that abnormal expression of S100A1 is strongly correlated with a number of severe human diseases: cardiomyopathy and neurodegenerative disorders. A few years ago we have found that thionylation of Cys 85 - the unique cysteine in two identical S100A1 subunits - leads to a drastic increase of the protein affinity for calcium. We postulated that the protein activated by thionylation becomes a more efficient calcium signal transmitter. Therefore, we decided to undertake, using NMR methods, a comparative study of structure and dynamics of native and thionylated human S100A1 in its apo and holo states. In this paper we present the results obtained for the both forms of this protein in its holo state and compare them with the previously published structure of native apo S100. The main conclusion that we draw from these results is that the increased calcium binding affinity of S100A1 upon thionylation arises, most probably, from rearrangement of the hydrophobic core in its apo form.
PMID: 23351007 [PubMed - as supplied by publisher]
Solution NMR structure and dynamics of human apo-S100A1 protein.
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J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
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[NMR paper] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d
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S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each...
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11-24-2010 08:49 PM
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A 7.6 ns molecular dynamics trajectory of the betaARK1 PH domain in explicit water with appropriate ions was calculated at 300 K. Spectral densities...
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[NMR paper] NMR-derived three-dimensional solution structure of protein S complexed with calcium.
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Authors: Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is...
Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics.
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