Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.

ABSTRACT: Transparency in the eye lens is maintained via specific, functional interactions among the structural βγ- and chaperone α-crystallins. Here, we report the structure and α-crystallin binding interface of the G18V variant of human γS-crystallin (γS-G18V), which is linked to hereditary childhood-onset cortical cataract. Comparison of the solution nuclear magnetic resonance structures of wild-type and G18V γS-crystallin, both presented here, reveal that the increased aggregation propensity of γS-G18V results from neither global misfolding nor the solvent exposure of a hydrophobic residue but instead involves backbone rearrangement within the N-terminal domain. αB-crystallin binds more strongly to the variant, via a well-defined interaction surface observed via chemical shift differences. In th

SUBMITTER: Kingsley CN 

PROVIDER: S-EPMC3940334 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature