The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture

Structure. 2011 Dec 7;19(12):1855-63. doi: 10.1016/j.str.2011.09.015.

Abstract

We report structural models for the most abundant oligomers populated by the polydisperse molecular chaperone αB-crystallin. Subunit connectivity is determined by using restraints obtained from nuclear magnetic resonance spectroscopy and mass spectrometry measurements, enabling the construction of various oligomeric models. These candidate structures are filtered according to their correspondence with ion-mobility spectrometry data and cross-validated by using electron microscopy. The ensuing best-fit structures reveal the polyhedral architecture of αB-crystallin oligomers, and provide a rationale for their polydispersity and facile interconversion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Models, Molecular
  • Protein Structure, Quaternary
  • alpha-Crystallin B Chain / chemistry*

Substances

  • alpha-Crystallin B Chain