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X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins

Bax, Benjamin ORCID:, Lapatto, R., Nalini, V., Driessen, H., Lindley, P. F., Mahadevan, D., Blundell, T. L. and Slingsby, C. 1990. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins. Nature 347 (6295) , pp. 776-780. 10.1038/347776a0

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THE β, γ-crystallins form a class of homologous proteins in the eye lens. Each γ-crystallin comprises four topologically equivalent, Greek key motifs; pairs of motifs are organized around a local dyad to give domains and two similar domains are in turn related by a further local dyad1–4. Sequence comparisons and model building predicted that hetero-oligomeric β-crystallins also had internally quadruplicated subunits, but with extensions at the N and C termini, indicating that β, γ-crystallins evolved in two duplication steps from an ancestral protein folded as a Greek key5–7. We report here the X-ray analysis at 2.1 Å resolution of βB2-crystall in homodimer which shows that the connecting peptide is extended and the two domains separated in a way quite unlike γ-crystallin. Domain interactions analogous to those within monomeric γ-crystallin are intermolecular and related by a crystallographic dyad in the βB2-crystallin dimer. This shows how oligomers can evolve by conserving an interface rather than connectivity. A further interaction between dimers suggests a model for more complex aggregates of β-crystallin in the lens

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Nature Publishing Group
ISSN: 0028-0836
Last Modified: 23 Oct 2022 14:03

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