Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach.

ABSTRACT: The molecular chaperone αB-crystallin, the major player in maintaining the transparency of the eye lens, prevents stress-damaged and aging lens proteins from aggregation. In nonlenticular cells, it is involved in various neurological diseases, diabetes, and cancer. Given its structural plasticity and dynamics, structure analysis of αB-crystallin presented hitherto a formidable challenge. Here we present a pseudoatomic model of a 24-meric αB-crystallin assembly obtained by a triple hybrid approach combining data from cryoelectron microscopy, NMR spectroscopy, and structural modeling. The model, confirmed by cross-linking and mass spectrometry, shows that the subunits interact within the oligomer in different, defined conformations. We further present the molecular architectures of additiona

SUBMITTER: Braun N 

PROVIDER: S-EPMC3251151 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature