Abstract
Parvalbumin (PA) is a classical small, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily expressed in vertebrates in a tissue- and cell-specific manner, serving as a magnesium/ calcium buffer. In the last decade novel data were published on structural peculiarities of PA, likely affecting its functionality. This review sums up these findings and discusses their potential physiological significance.
Keywords: Parvalbumin, oncomodulin, metal binding, protein unfolding, protein isoforms, structural microheterogeneity, intrinsically disordered protein, antioxidant activity, allergen.
Graphical Abstract
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