Parvalbumin as a Pleomorphic Protein

Curr Protein Pept Sci. 2017;18(8):780-794. doi: 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.

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

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Calcium / chemistry*
  • Calcium / metabolism
  • Carps
  • Humans
  • Intrinsically Disordered Proteins
  • Ion Transport
  • Magnesium / chemistry*
  • Magnesium / metabolism
  • Models, Molecular
  • Parvalbumins / chemistry*
  • Parvalbumins / genetics
  • Parvalbumins / metabolism
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Protein Structure, Tertiary

Substances

  • Intrinsically Disordered Proteins
  • Parvalbumins
  • Protein Isoforms
  • Magnesium
  • Calcium