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The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II

Nature volume 289, pages 771–777 (1981)Cite this article

Abstract

The three-dimensional structure of the eye lens protein, bovine γ-crystallin II, has been determined at 2.6 Å resolution. The protein has a two domain β-structure, folded into four remarkably similar ‘Greek 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 intermodular cross-linking leading to aggregation, both of which may be important in cataract formation.

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Author information

Affiliations

  1. Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, University of London, London, WC1E 7HX, UK

    Tom Blundell, Peter Lindley, Linda Miller, David Moss, Christine Slingsby, Ian Tickle, Bill Turnell & Graeme Wistow

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  1. Tom Blundell
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  2. Peter Lindley
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  3. Linda Miller
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  4. David Moss
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  5. Christine Slingsby
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  6. Ian Tickle
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  7. Bill Turnell
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  8. Graeme Wistow
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Blundell, T., Lindley, P., Miller, L. et al. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II. Nature 289, 771–777 (1981). https://doi.org/10.1038/289771a0

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