The molecular structure and stability of the eye lens: x-ray analysis of gamma-crystallin II

Nature. 1981 Feb 26;289(5800):771-7. doi: 10.1038/289771a0.


The three-dimensional structure of the eye lens protein, bovine gamma-crystallin II, has been determined at 2.6 A resolution. The protein has a tow domain beta-structure, folded into four remarkably similar 'Greed key' motifs, and shows the highest internal symmetry of any protein studied by X-ray analysis. Although the symmetrical structure seems very stable, the arrangement of the sulphydryl groups would allow intramolecular cross-linking leading to possible destabilization, and intermolecular cross-linking leading to aggregation, both of which may be important to cataract formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Evolution
  • Cattle
  • Crystallins* / genetics
  • Cysteine
  • Genes
  • Lens, Crystalline / metabolism*
  • Protein Conformation
  • Surface Properties
  • X-Ray Diffraction


  • Crystallins
  • Cysteine