Letter to the Editor: 1H, 15N and 13C resonance assignments of rabbit apo-S100A11 |
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| Authors: | Anne C. Rintala Brett O. Schönekess Michael P. Walsh Gary S. Shaw |
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| Affiliation: | (1) Department of Biochemistry and McLaughlin Macromolecular Structure Facility, University of Western Ontario, London, Ontario, Canada, N6A 5C1;(2) Smooth Muscle Research Group and CIHR Group in Regulation of Vascular Contractility, Department of Biochemistry & Molecular Biology, University of Calgary, Faculty of Medicine, 3330 Hospital Drive N.W., Calgary, Alberta, Canada, T2N 4N1 |
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| Abstract: | S100 proteins belong to the EF-hand family of calcium binding proteins. Upon calcium binding, these proteins undergo a conformational change to expose a hydrophobic region necessary for target protein interaction. One member of the S100 protein family is S100A11, first isolated from chicken gizzard and termed calgizzarin. It was later isolated from other organisms and tissues including human placenta, pig heart and rabbit lung. The physiological target of S100A11 is thought to be annexin I, a phospholipid-binding protein involved in EGF receptor sorting. This work reports the 1H, 15N and 13C resonance assignments of rabbit apo-S100A11 determined using 15N, 13C-labelled protein and multidimensional NMR spectroscopy. |
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| Keywords: | rabbit S100A11 resonance assignments |
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