¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V

Biomol NMR Assign. 2012 Apr;6(1):63-7. doi: 10.1007/s12104-011-9326-1. Epub 2011 Jul 7.

Abstract

We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone variants will advance understanding of cataract formation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cataract / genetics*
  • Humans
  • Hydrogen-Ion Concentration
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • Mutation*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Conformation
  • Temperature
  • gamma-Crystallins / chemistry*
  • gamma-Crystallins / genetics*

Substances

  • gamma-Crystallins
  • CRYGS protein, human