AI Article Synopsis

  • γS-crystallin is crucial for eye lens stability and has little turnover, with the G57W mutant linked to congenital cataracts.
  • Researchers cloned and purified the γS-G57W protein to study its structure.
  • The findings include detailed resonance assignments for the mutant protein using advanced NMR techniques, showing it has an ordered conformation.

Article Abstract

γS-crystallin is a major structural component of the human eye lens, which maintains its stability over the lifetime of an organism with negligible turnover. The G57W mutant of human γS-crystallin (abbreviated hereafter as γS-G57W) is associated with dominant congenital cataracts. In order to provide a structural basis for the ability of γS-G57W causing cataract, we have cloned, overexpressed, isolated and purified the protein. The 2D [N-H]-HSQC spectrum recorded with uniformly C/N-labelled γS-G57W was highly dispersed indicating the protein to adopt an ordered conformation. In this paper, we report almost complete sequence-specific H, C and N resonance assignments of γS-G57W using a suite of heteronuclear 3D NMR experiments.

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http://dx.doi.org/10.1007/s12104-017-9779-yDOI Listing

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