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.
Current Protein & Peptide Science
Title:Parvalbumin as a Pleomorphic Protein
Volume: 18 Issue: 8
Author(s): Eugene A. Permyakov*, Vladimir N. Uversky and Sergei E. Permyakov
Affiliation:
- Institute for Biological Instrumentation of the Russian Academy of Sciences, Institutskaya str., 7, Pushchino, Moscow region 142290,Russian Federation
Keywords: Parvalbumin, oncomodulin, metal binding, protein unfolding, protein isoforms, structural microheterogeneity, intrinsically disordered protein, antioxidant activity, allergen.
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.
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Cite this article as:
Permyakov A. Eugene*, Uversky N. Vladimir and Permyakov E. Sergei, Parvalbumin as a Pleomorphic Protein, Current Protein & Peptide Science 2017; 18 (8) . https://dx.doi.org/10.2174/1389203717666161213115746
DOI https://dx.doi.org/10.2174/1389203717666161213115746 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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