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Parvalbumin as a Pleomorphic Protein.

Eugene A Permyakov1, Vladimir N Uversky2, Sergei E Permyakov3

  • 1Institute for Biological Instrumentation of the Russian Academy of Sciences, Institutskaya str., 7, Pushchino, Moscow region 142290, Russian Federation.

Current Protein & Peptide Science
|December 15, 2016
PubMed
Summary

Parvalbumin, a calcium-binding protein, has unique structural features that may influence its function. This review explores these recent findings and their physiological importance.

Keywords:
Parvalbuminallergenantioxidant activityintrinsically disordered proteinmetal bindingoncomodulinprotein isoformsprotein unfoldingstructural microheterogeneity

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Parvalbumin (PA) is a small, cytosolic calcium-binding protein belonging to the EF-hand superfamily.
  • PA is expressed in a tissue- and cell-specific manner across vertebrates.
  • Its primary known function is as a magnesium/calcium buffer.

Purpose of the Study:

  • To review recent findings on structural peculiarities of Parvalbumin.
  • To discuss the potential physiological significance of these structural variations.

Main Methods:

  • Literature review of recent studies on Parvalbumin structure and function.

Main Results:

  • Novel structural characteristics of Parvalbumin have been identified.
  • These structural peculiarities may impact PA's buffering capacity and interactions.

Conclusions:

  • Recent structural data suggest a more complex role for Parvalbumin beyond simple calcium buffering.
  • Understanding these structural nuances is crucial for elucidating PA's full physiological significance.