The molecular structure and stability of the eye l...[Nature. 1981]

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1: Nature. 1981 Feb 26;289(5800):771-7.Links

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

Blundell T, Lindley P, Miller L, Moss D, Slingsby C, Tickle I, Turnell B, Wistow G.

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.

PMID: 7464942 [PubMed - indexed for MEDLINE]

X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution. [J Mol Biol. 1983]
High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin. [J Mol Biol. 1991]
Packing interactions in the eye-lens. Structural analysis, internal symmetry and lattice interactions of bovine gamma IVa-crystallin. [J Mol Biol. 1989]
ReviewProbing the structure and interactions of crystallin proteins by NMR spectroscopy. [Prog Retin Eye Res. 1999]
ReviewLens crystallins of invertebrates--diversity and recruitment from detoxification enzymes and novel proteins. [Eur J Biochem. 1996]

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

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