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
Keywords: Parvalbumin, oncomodulin, metal binding, protein unfolding, protein isoforms, structural microheterogeneity,
intrinsically disordered protein, antioxidant activity, allergen.
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