Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation.

ABSTRACT:

Background

Lens transparency is due to the ordered arrangement of the major structural proteins, called crystallins. βB2 crystallin in the lens of the eye readily forms dimers with other β-crystallin subunits, but the resulting heterodimer structures are not known and were investigated in this study.

Methods

Structures of βA3 and βB2 crystallin homodimers and the βA3/βB2 crystallin heterodimers were probed by measuring changes in solvent accessibility using hydrogen-deuterium exchange with mass spectrometry. We further mimicked deamidation in βB2 and probed the effect on the βA3/βB2 heterodimer. Results were confirmed with chemical crosslinking and NMR.

Results

Both βA3 and βB2 had significantly decreased deuterium levels in the heterodimer compared to their respectiv

SUBMITTER: Lampi KJ 

PROVIDER: S-EPMC4673030 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature