1oki
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CRYSTAL STRUCTURE OF TRUNCATED HUMAN BETA-B1-CRYSTALLIN
OverviewOverview
Crystallins are long-lived proteins packed inside eye lens fiber cells, that are essential in maintaining the transparency and refractive power of, the eye lens. Members of the two-domain betagamma-crystallin family, assemble into an array of oligomer sizes, forming intricate higher-order, networks in the lens cell. Here we describe the 1.4 angstroms resolution, crystal structure of a truncated version of human betaB1 that resembles an, in vivo age-related truncation. The structure shows that unlike its close, homolog, betaB2-crystallin, the homodimer is not domain swapped, but its, domains are paired intramolecularly, as in more distantly related, monomeric gamma-crystallins. However, the four-domain dimer resembles one, half of the crystallographic bovine betaB2 tetramer and is similar to the, engineered circular permuted rat betaB2. The crystal structure shows that, the truncated betaB1 dimer is extremely well suited to form higher-order, lattice interactions using its hydrophobic surface patches, linker, regions, and sequence extensions.
DiseaseDisease
Known disease associated with this structure: Cataract, pulverulent OMIM:[600929]
About this StructureAbout this Structure
1OKI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of truncated human betaB1-crystallin., Van Montfort RL, Bateman OA, Lubsen NH, Slingsby C, Protein Sci. 2003 Nov;12(11):2606-12. PMID:14573871
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