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.
Peptide binding proclivities of calcium loaded calbindin-D28k
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. https://doi.org/10.1016/j.febslet.2007.09.004