Peptide binding proclivities of calcium loaded calbindin-D28k
Calbindin-D28k is known to function as a calcium-buffering protein in the cell. Moreover, recent evidence shows that it also plays a role as a sensor. Using circular dichroism and NMR, we show that calbindin-D28k undergoes significant conformational changes upon binding calcium, whereas only minor changes occur when binding target peptides in its Ca2+ -loaded state. NMR experiments also identify residues that undergo chemical shift changes as a result of peptide binding. The subsequent use of computational protein-protein docking protocols produce a model describing the interaction interface between calbindin-D28k and its target peptides. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Kordys, D. R., Bobay, B. G., Thompson, R. J., Venters, R. A., & Cavanagh, J. (2007). Peptide binding proclivities of calcium loaded calbindin-D28k. FEBS Letters, 581(24), 4778-4782. DOI: 10.1016/j.febslet.2007.09.004