Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2049588 | FEBS Letters | 2007 | 5 Pages |
Abstract
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.
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Authors
David R. Kordys, Benjamin G. Bobay, Richele J. Thompson, Ronald A. Venters, John Cavanagh,