Parvalbumin as a Pleomorphic Protein

Document Type

Article

Publication Date

2017

Keywords

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

Digital Object Identifier (DOI)

https://doi.org/10.2174/1389203717666161213115746

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.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Current Protein & Peptide Science, v. 18, issue 8, p. 780-794

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