Bax, Benjamin  ORCID: https://orcid.org/0000-0003-1940-3785, 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
|
Abstract
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: | Schools > Biosciences |
| Publisher: | Nature Publishing Group |
| ISSN: | 0028-0836 |
| Last Modified: | 23 Oct 2022 14:03 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/112655 |
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