ArticleProtein science : a publication of the Protein Society1997
The X-ray structure of a mutant eye lens beta B2-crystallin with truncated sequence extensions.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 25 citations in OpenAlex.
- Whole Exome Sequencing Reveals a Mutation in CRYBB2 in a Large Mexican Family with Autosomal Dominant Pulverulent Cataract.Molecular syndromology · 2016Article
- Evolution of crystallins for a role in the vertebrate eye lens.Protein science : a publication of the Protein Society · 2013Review
- A missense mutation in CRYBA4 associated with congenital cataract and microcornea.Molecular vision · 2010Article
- Mitochondrial proteomics in experimental autoimmune uveitis oxidative stress.Investigative ophthalmology & visual science · 2009Article
- N-terminal extension of beta B1-crystallin: identification of a critical region that modulates protein interaction with beta A3-crystallin.Biochemistry · 2009Article
- Mutation analysis of congenital cataract in a Basotho family identified a new missense allele in CRYBB2.Molecular vision · 2009Article
- Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.Protein science : a publication of the Protein Society · 2007Article
- CRYBA4, a novel human cataract gene, is also involved in microphthalmia.American journal of human genetics · 2006Article
- Gamma-D crystallin gene (CRYGD) mutation causes autosomal dominant congenital cerulean cataracts.Journal of medical genetics · 2003Article
- A nonsense mutation in CRYBB1 associated with autosomal dominant cataract linked to human chromosome 22q.American journal of human genetics · 2002Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
beta-Crystallins are oligomeric eye lens proteins that are related to monomeric gamma-crystallins by domain swapping: like gamma-crystallins, they are comprised of two similar domains but they differ in having long sequence extensions. beta B2, a major component of beta-crystallin oligomers, self-associates to a homodimer in solution. In two crystal structures of native beta B2, the protein is a 222-symmetric tetramer of eight domains. It has previously been shown that a mutant of rat beta B2-crystallin, in which the bulk of the N- and C-terminal sequence extensions has been deleted, assembles into dimers and tetramers. Here we present the 3.0 A resolution X-ray structure of the tetramer, beta B2 delta NC1. The mutant tetramer has a very similar set of domain interactions to the native structure. However, the structures differ in the relative orientation of the two sets of four domains. The paired N- and C-terminal domain interface, which is at the heart of the dimer structure, is very similar to the native structure. However, the truncation of the C-terminal extension removes an important tryptophan residue, which prevents the extension from acting as a (non-covalent) linker, as it does in native beta B2. There is a knock-on structural effect that removes a contact between extension and covalent linker, and this appears to cause a small twist in the linker that is amplified into a 20 degrees rotation between sets of paired domains.
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