1OKI
Crystal structure of truncated human beta-B1-crystallin
Summary for 1OKI
| Entry DOI | 10.2210/pdb1oki/pdb |
| Descriptor | BETA CRYSTALLIN B1 (2 entities in total) |
| Functional Keywords | crystallin, cataract, eye lens protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 2 |
| Total formula weight | 48504.18 |
| Authors | van Montfort, R.L.M.,Bateman, O.A.,Lubsen, N.H.,Slingsby, C. (deposition date: 2003-07-25, release date: 2004-01-22, Last modification date: 2024-11-06) |
| Primary citation | Van Montfort, R.L.M.,Bateman, O.A.,Lubsen, N.H.,Slingsby, C. Crystal Structure of Truncated Human Beta-B1-Crystallin Protein Sci., 12:2606-, 2003 Cited by PubMed Abstract: 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. PubMed: 14573871DOI: 10.1110/PS.03265903 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
